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Plasmafraktionierung

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Transfusionsmedizin

Zusammenfassung

Das menschliche Blutplasma enthält mehr als 120 heute bekannte Proteine. Mit Hilfe der Plasmafraktionierung in großtechnischem Maßstab wird versucht, einzelne Eiweißfraktionen für den therapeutischen Einsatz bei Patienten mit fehlenden oder funktionell defekten Plasmaproteinen herzustellen. So gewonnene Plasmaderivate sind v. a. bei Gerinnungsstörungen, Eiweißmangel und Antikörpermangelsyndromen von Bedeutung. Manche Plasmaproteine lassen sich inzwischen auch gentechnisch herstellen. Es ist zu erwarten, daß mit der zunehmenden Kenntnis der Funktion weiterer Plasmaproteine und den Möglichkeiten zu ihrer gentechnischen Produktion deren Einsatz eine enorme Ausweitung erfahren wird.

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Literatur

  1. Allen RH, Majerus PW (1972) Isolation of vitamin B„-binding protein using affinity chromatography. III. Purification and properties of human plasma Transcobalamin II J Biol Chem 247: 7709–7717

    Google Scholar 

  2. Amann E, Abel KJ, Grundmann U, Okazaki H, Küpper HA (1988) Synthesis of human factor XIIIa in bacterial cells. Behring Inst Mitt 82: 35–42

    Google Scholar 

  3. Anson DS, Austen DE, Brownlee GG (1985) Expression of active human clotting factor IX from recombinant DNA clones in mammalian cells. Nature (London) 315: 683–685

    CAS  Google Scholar 

  4. Arnaud P, Gianazza E (1984) Alpha,-Antitrypsin-Protease Interactions: The Biological Aspect. In: Arnaud P, Benvenu J, Laurant P (eds) Marker proteins inflammatory, vol 2. De Gruyter, Berlin New York, pp 181–201

    Google Scholar 

  5. Auerswald G, Novakovä-Banet A, Heimburger N, Popp M (1984) New pasteurised factor IX concentrate: Manufacturing. Clinical efficacy and hepatitis-safety. XVI Int Congr World Federation of Hemophilia, Rio de Janeiro (Brazil), 24.-28. Aug. 1984

    Google Scholar 

  6. Barrowcliffe TW, Stableforth P, Dormandy KM (1973) Small scale preparation and clinical use of factor IX-prothrombin complex. Vox Sang 25: 426–441.

    Google Scholar 

  7. Berggärd J (1965) Identification and isolation of urinary proteins. In: Peeters H (ed) Protides of the biological fluids: Proc 12t Col Bruges, 1964, pp 285–291

    Google Scholar 

  8. Berkner K, Busby S, Davie EW, Hart C, Insley M (1986) Isolation and expression of cDNA encoding human factor VII. Cold Spring Harbor Symp Quant Biol LI: 531–541

    Google Scholar 

  9. Bhakdi S, Tranum-Jensen J (1983) Membrane damage by complement. Biochim Biophys Acta 737: 343–372

    Google Scholar 

  10. Bhakdi S, Tranum-Jensen J (1984) Mechanism of complement cytolysis and the concept of channel-forming proteins. Philos Trans R Soc London Ser B 306: 311–324

    CAS  Google Scholar 

  11. Bier M (1957) New Principle of preparative electrophoresis. Science 125: 1084–1085

    PubMed  CAS  Google Scholar 

  12. Bing DH, Andrews JM, Morris KM, Cole E, Irish V (1980) Purification of subcomponents C1q, Cir and Cis of the first component of complement from Cohn fraction I by affinity chromatography. Prep Biochem 10: 269–296

    PubMed  CAS  Google Scholar 

  13. Björling H (1972) Plasma Fractionation Methods Used in Sweden. Vox Sang 23: 18–25

    PubMed  Google Scholar 

  14. Blombäck B, Blombäck M (1956) Purification of human and bovine fibronogen. Ark Kemi 10: 415–443

    Google Scholar 

  15. Blombäck M (1958) Purification of antihemophilic globulin. Ark Kemi 12: 387–396

    Google Scholar 

  16. Blundell TL, Johnson LN (eds) (1976) Protein crystallography. Academic Press. New York London San Francisco

    Google Scholar 

  17. Brackmann HH, Egli H (1988) Acute hepatitis B infection after treatment with heat-inactivated factor VIII concentrate. Lancet 2: 967 (letter)

    Google Scholar 

  18. Brinkhous KM, Shanbrom E, Robert HR, Webster WP, Fekete L, Wagner RH (1968) A New High-Potency Glycine-Precipitated Antihemophilic Factor (AHF) Concentrate. JAMA 205: 67–71

    Google Scholar 

  19. Bröker M, Ragg H, Karges HE (1987) Expression of human antithrombin III in saccharomyces cerevisiae and schizosaccharomyces pombe. Biochim Biophys Acta 908: 203–213

    PubMed  Google Scholar 

  20. Bröker M, Karges HE (1988) Expression of human factor XIIIa in yeast. Yeast 4: 142

    Google Scholar 

  21. Bürgi W, Schmid K (1961) Preparation and properties of Znaz glycoprotein of normal human plasma. J Biol Chem 236: 1066–1074

    PubMed  Google Scholar 

  22. Burstein M, Scholnick HR, Mortin R (1970) Rapid method for the isolation of lipoproteins from human serum by precipitation with polyanions. J Lipid Res 11: 583–595

    Google Scholar 

  23. Busby S, Kumar A, Joseph M et al. (1985) Expression of active human factor IX in transfected cells. Nature (London) 316: 271–273

    CAS  Google Scholar 

  24. Carlebjörk G, Blombäck M, Akerblom 0 (1983) Improvement of Plasma Quality as Raw Material for Factor VIII: C Concentrates. Vox Sang 45: 233–242

    Google Scholar 

  25. Casper CK, Lusher JM, Silberstein LE, Anderson KC, Goodnough LT et al. (1993) Recent revolution of clotting factor concentrates for hemophilia A and B. Transfusion 33: 422–434

    Google Scholar 

  26. Chanutin A, Curnish RR (1960) The precipitation of plasma proteins by short chain fatty acids. Arch Biochem Biophys 89: 218–220

    PubMed  CAS  Google Scholar 

  27. Charm SE, Landau S, Williams B, Horowitz B, Prince AM, Pascual D (1992) High temperature short-time heat inactivation of HIV and other viruses in human blood plasma. Vox Sang 62: 12–20

    PubMed  CAS  Google Scholar 

  28. Cohn EJ (1953) A chemical prologue on the characterization and separation of proteins by virtue of their interactions with neutral salts. In: Tullis JL (ed) Blood cells and plasma proteins: Their state in nature. Academic Press, New York, pp 18–28

    Google Scholar 

  29. Cohn EJ, Luetscher AJ jr, Oncley JL, Armstrong SJ jur, Davis DB (1940) Preparation and Properties of serum and plasma proteins. III. Size and charge of proteins separating upon equilibration across membranes with ethanol-water mixtures of controlled pH, ionic strength and temperature. J Am Chem Soc 62: 3396–3400

    Google Scholar 

  30. Cohn EJ, Strong LE, Hughes WL jr, Mulford DJ, Ashworth JN, Melin M, Taylor HL (1946) Preparation and properties of serum and plasma proteins. IV. A system for the separation into fractions of the protein and lipoprotein components of biological tissues and fluids. J Am Chem Soc 68: 459–475

    Google Scholar 

  31. Cohn EJ, Gurd FRN, Surgenor DM, Barnas AB, Brown RK, Derouaux G, Gillespie JM, Kahnt FW, Lever WF, Lui CH, Mittelman D, Mouton RF, Schmid K, Uroma E (1950) A System for the separation of the components of human blood: Quantitative procedures for the separation of the protein components of human plasma. J Am Chem Soc 72: 465–474

    Google Scholar 

  32. Curling JM (1980) Methods of plasma protein fractionation. Academic Press, London

    Google Scholar 

  33. Davis SG, Sim RG (1981) Intramolecular general acid catalysis in the binding reactions of af macroglobulin and complement components C3 and C4. Biosci Rep 1: 461–468

    Google Scholar 

  34. De Biasi R, Rocino A, Miraglia E, Mastrullo R, Quirino A (1992) The impact of a very high purity factor VIII concentrate on the immune system of human immunodeficiency virus-infected hemophiliacs: A randomized prospective, two-year comparison with an intermediate purity concentrate. Blood 78: 1919–1922

    Google Scholar 

  35. Deutsch DG, Mertz ET (1970) Plasminogen: Purification from human plasma by affinity chromatography. Science 170: 1095–1096

    PubMed  CAS  Google Scholar 

  36. Deutsch HF, Gosting LJ, Alberty RA, Williams JW (1946) Biophysical studies of blood plasma proteins. III. Recovery of y -Globulin from human blood protein mixtures. J Biol Chem 164: 109–118

    PubMed  CAS  Google Scholar 

  37. Dietzel E, Geiger H (1964) Gewinnung and Eigenschaften therapeutisch wichtiger Human-Plasmaproteine. Behringwerk-Mitt 43: 129–159

    Google Scholar 

  38. Dike GWR, Bidwell E, Rizza CR (1972) The preparation and clinical use of a new concentrate containing factor IX, pro-thrombin and factor X and a separate concentrate containing factor VII. Br J Haematol 22: 469–490

    PubMed  CAS  Google Scholar 

  39. Dileo AJ, Allegrezza AE, Builder SE (1992) High resolution removal of virus from protein solutions using a membran of unique structure. Bio/Technology to: 182–188

    Google Scholar 

  40. Edsall JT (1947) The Plasma Protein and Their Fractionation. Adv Protein Chem 3: 383–479

    Google Scholar 

  41. Ek K, Bjellqvist B, Righetti PG (1983) Preparative isoelectric focusing in immobilized pH gradients. I. General principle and methodology. J Biochem Biophys Meth 8: 135–155

    Google Scholar 

  42. Eschholz WM (1985) Präparative Einflüsse auf die Gerinnungsaktivität von fresh frozen Plasma. Med Diss, Univ Marburg

    Google Scholar 

  43. Fex G, Laurell CB, Thulin E (1977) Purification of prealbumin from human and canine serum using a two-step affinity chromatographic procedure. Eur J Biochem 75: 181–186

    PubMed  CAS  Google Scholar 

  44. Fine JM, Steinbuch M (1970) A simple technique for the isolation of monoclonal IgG and IgA. Rev Eur Etudes Clin Biol XV: 1115–1121

    Google Scholar 

  45. Foster D, Davie EW (1984) Charaterization of a cDNA coding for human protein C. Proc Natl Acad Sci USA 81: 4766–4770

    PubMed  CAS  Google Scholar 

  46. Foukal Z, Prosek J, Veprekova A (1956) Die Gamma-Globulin Fabrikation in der Tschechoslowakei nach der modifizierten to. Cohn’schen Fraktionierungsmethode. Experientia 12: 402–404

    PubMed  CAS  Google Scholar 

  47. Fuhge P, Gratz P, Geiger H (1986) Moderne Methoden zur Herstellung von Gerinnungstherapeutika. Behring Inst Mitt

    Google Scholar 

  48. Gellis 79: S, N164–176eefe J, Strong L et al. (1948) Chemical, clinical and immunological studies on products of human plasma fractionation: Inactivation of virus of homologous serum albumin by means of heat. J Clin Invest 27: 239–244

    Google Scholar 

  49. Gitschier J, Wood WI, Goralka TM, Wion KL, Chen EY, Eaton DH, Vehar GA, Capon DJ, Lawn RM (1984) Characterization of the human factor VIII gene. Nature (London) 312: 326–330

    CAS  Google Scholar 

  50. Gofman JW, Lindgren IT, Elliot H (1949) Ultracentrifugal studies of lipoproteins of human serum. J Biol Chem 179: 973–979

    PubMed  CAS  Google Scholar 

  51. Grassmann W, Hannig K (1950) Ein einfaches Verfahren zur Analyse der Serumproteine und anderer Proteingemische. Naturwissenschaften 37: 496–497

    Google Scholar 

  52. Grassmann W, Hannig K (1958) Präparative Elektrophorese. In: Müller E (Hrsg) Houben-Weyl, Methoden der organischen Chemie, BdL/i. Thieme, Stuttgart, pp 680–751

    Google Scholar 

  53. Grundmann U, Amann E, Zettlmeissl G, Köpper HA (1986) Characterization of cDNA coding for human factor XIII a. Proc Natl Acad Sci USA 83: 8024–8028

    PubMed  CAS  Google Scholar 

  54. Gürtler L (1994) Nebenwirkungen der Substitutionstherapie. Virologische Aspekte. Haemostaseologie 14: 55–59

    Google Scholar 

  55. Hardy WB, Gardiner S (1910) Proteins of blood plasma. J Physiol (London) 40: LXVIII-LXXI.

    Google Scholar 

  56. Harrison RA (1983) Human Cl inhibitor: improved isolation and preliminary structural characterization. Biochemistry 22: 5001–5007

    PubMed  CAS  Google Scholar 

  57. Haupt H (1990) Chemie und klinische Bedeutung der Human-Plasmaproteine. Behring Inst Mitt 86: 1–66

    PubMed  CAS  Google Scholar 

  58. Haupt H, Baudner S (1981) Isolierung und Kristallisation der Human-Komplement-Subkomponente Cir des C1-Komplexes. Hoppe Seyler’s Z Physiol Chem 362: 1147–1150

    PubMed  CAS  Google Scholar 

  59. Haupt H, Heide K (1967) Kristallisation von Human-Albumin mit Mineralsalzen. Klin Wochenschr 45: 726–729

    Google Scholar 

  60. Haupt H, Heide K ( 1969 Kristallisation des mit Plasmin erhaltenen Fc-Fragment aus Human-IgG-Globulin. Klin Wochenschr 47: 270–272

    PubMed  CAS  Google Scholar 

  61. Haupt H, Heide K, Zwisler O, Schwick HG (1966) Isolierung und physikalisch-chemische Charakterisierung der Cholinesterase aus Humanserum. Blut XIV: 65–75

    Google Scholar 

  62. Haupt H, Heide K, Schwick HG (1970) Isolierung und Kristallisation von,E-Globulin aus Humanserum. Klin Wochenschr 48: 550–552

    Google Scholar 

  63. Haupt H, Heimburger N, Kranz T, Schwick HG (1970) Ein Beitrag zur Isolierung und Charakterisierung des Cl-Inaktivators aus Humanplasma. Eur J Biochem 17: 254–261

    PubMed  CAS  Google Scholar 

  64. Haupt H, Heide K, Schwick HG (1973) Kristallisation von Human-Blutproteinen. Leitz-Mitt VI: 59–64

    Google Scholar 

  65. Hedner U, Glazer S, Dingei K, Alberts KA, Blombäck M, Schulman S, Johnson H (1988) Successful use of recombinant factor VIIa in patient sites severe haemosphilia A during synovectomy. Lancet II: 1193

    Google Scholar 

  66. Heide K, Haupt H (1964) Darstellung noch nicht therapeutisch angewandter Plasmaproteine. Behringwerk-Mitt 43: 161–193

    Google Scholar 

  67. Heide K, Haupt H, Schwick HG (1977) Plasma Protein Fractionation. In: Putnam FW (ed) The plasma proteins, vol III. Academic Press. New York San Francisco London, pp 545–597

    Google Scholar 

  68. Heimburger N, Schwick HG (1968) Charakterisierung und Isolierung von Proteinen durch Elektrophoresemethoden. IV Int Symp Chromatographie Electrophorese. Press Acad Eur, Bruxelles 1968, pp 39–61

    Google Scholar 

  69. Heimburger N, Haupt H, Schwick HG (1971) Proteinase inhibitors of human plasma. Proc Int Res Conf Proteinase Inhibitors, Munich Nov 1970, pp 1–21

    Google Scholar 

  70. Heimburger N, Schwinn H, Gratz P, Lüben G, Kumpe G, Herchenhan B (1981) Faktor VIII-Konzentrat, hochgereinigt und in Lösung erhitzt. Arzneimittelforschung 31: 619–622

    PubMed  CAS  Google Scholar 

  71. Heimburger N, Karges H, Weidmann E (1987) Virus safety of pasteurized factor VIII and factor IX concentrates: Study in virgin patients. Dev Biol Stand 67: 303–310

    PubMed  CAS  Google Scholar 

  72. Heimburger N (1991) Herstellung virusinaktivierter Gerinnungsfaktor-Konzentrate. Med Welt 42: 628–632

    Google Scholar 

  73. Himmelhoch SR (1971) Chromatography of proteins on ion-exchange adsorbents. Meth Enzymol 22: 273–286

    Google Scholar 

  74. Hjelm H, Hjelm K, Sjöquist J (1972) Protein A from staphylococcus aureus. Its isolation by affinity chromatography and its use as an immunosorbent for isolation of immunoglobulins. FEBS Lett 28: 73–76

    PubMed  CAS  Google Scholar 

  75. Hjertén S (1975) Free displacement electrophoresis (isotachophoresis). In: Peeters H (ed) Protides of the biological fluids. Proc 22íh Col Brugge 1974: vol 22, pp 669–672

    Google Scholar 

  76. Hjertén S (1976) Hydrophobic interaction chromatography of proteins on neutral adsorbents. In: Catsimpoolas N (ed) Methods of protein separation, vol n. Plenum, New York pp 233–243

    Google Scholar 

  77. Hjertén S, Rosengren J, Pahlman S (1974) Hydrophobic interaction chromatography. The synthesis and the use of some alkyl and aryl derivatives of agarose. J Chromatogr 101: 281–288

    Google Scholar 

  78. Hoch J, Chanutin A (1954) Albumin from heated human plasma. I. Preparation and electrophoretic properties. Arch Biochem Biophys 51: 271–276

    PubMed  CAS  Google Scholar 

  79. Horejsi J, Smetana R (1954) The effect of Rivanol on plasma proteins. Collection Czech Chem Commun 19: 1316–1323

    Google Scholar 

  80. Horejsi J, Smetana R (1956) The isolation of y -globulin by rivanol. Acta Med Scand 155: 65–70

    PubMed  CAS  Google Scholar 

  81. Horowitz B, Wiebe ME, Lippin A et al. (1985) Inactivation of viruses in labile blood derivatives. I. Disruption of lipid-enveloped viruses by tri(n-butyl)phosphate detergent combinations. Transfusion 25: 516–522

    PubMed  CAS  Google Scholar 

  82. Hoyer LW (1981) The factor VIII complex: structure and function. Blood 58: 1–13

    PubMed  CAS  Google Scholar 

  83. Iwarson S, Kjellman H, Teger-Nilsson AC (1976) Incidence of viral hepatitis after administration of factor IX concentrates. Vox Sang 31: 136–140

    PubMed  CAS  Google Scholar 

  84. Johnson AJ, MacDonald VE, Brind J (1979) Enhanced yield of antihemophilic factor and von Willibrand factor by cryoprecipitation with polyethylene glycol. Vox Sang 36: 72–76

    PubMed  CAS  Google Scholar 

  85. Kägedal B, Kallberg M (1977) An improved procedure for the isolation of thyroxine-binding globulin from human pregnancy serum. Clin Chim Acta 78: 103–111

    PubMed  Google Scholar 

  86. Kakaiya RM, Morse EE, Panek S (1984) Labile coagulation factors in thawed fresh frozen plasma prepared by two methods. Vox Sang 46: 44–46

    Google Scholar 

  87. Kallee E, Lohss F, Oppermann W (1957) TrichloressigsäureAceton-Extraktion von Albumin aus Seren und Antigen-Antikörper-Präzipitaten. Z Naturforsch 12b: 777–783

    Google Scholar 

  88. Kaufman RJ, Wasley LC, Furie BC, Furie B, Shoemaker CB (1986) Expression, purification and characterization of recombinant and y-carboxylated factor IBC. Biol Chem 261: 9622–9628

    CAS  Google Scholar 

  89. Kaufman RJ, Wasley LC, Dorner AJ (1988) Synthesis, processing and secretion of recombinant human factor VIII expressed in mammalian cells. J Biol Chem 263: 6352–6362

    PubMed  CAS  Google Scholar 

  90. Kaufman RJ, Wasley LC, Davis MV et al. (1989) Effect of von Willebrand factor coexpression on the synthesis and secretion of factor VIII in chinese hamster ovary cells. Mol Cell Biol 9: 1233–1242

    PubMed  CAS  Google Scholar 

  91. Keilin D, Mann T (1940) Carbonic anhydrase. Purification and nature of the enzyme. Biochem J 34: 1163

    PubMed  CAS  Google Scholar 

  92. Kekwick RA, Mackay ME (1954)The separation of protein fractions from human plasma with ether. London. Her majesty’s stationery Office p 75 (Medical research council special report series, 286)

    Google Scholar 

  93. Kellner S, Stöcker U, Fürst G (1985) Untersuchungen zur Stabilität von Gerinnungsfaktoren im Plasma, eingefroren nach 6 und 18 Stunden nach Blutentnahme. Infusionstherapie 12: 208–210

    CAS  Google Scholar 

  94. Kisiel W, Hanahan DJ (1973) Purification and characterization of human factor II. Biochim Biophys Acta 304: 103–113

    PubMed  CAS  Google Scholar 

  95. Kistler P, Nitschmann H (1962) Large scale production of human plasma fractions. Vox Sang 7: 414–424

    PubMed  CAS  Google Scholar 

  96. Kistler P, Nitschmann H, Wyttenbach A, Studer M, Niederöst C, Mauerhofer M (1960) Humanes Siderophilin: Isolierung mittels Rivanol aus Blutplasma und Plasmafraktionen, analytische Bestimmung und Kristallisation. Vox Sang 5: 403–415

    Google Scholar 

  97. Klein JP, Bailly E, Schneweis KE, Brackmann HH, Hammerstein U, Haufland P, van de Loo B, Oldenburg J (1990) Acute HIV-1 infection in patients with hemophilia B treated with beta-propriolactone UV-inactivated clotting factor. Thromb Haemostas 64: 336–337 (letter)

    Google Scholar 

  98. Koerner K, Stampe D (1984) Die Stabilität von Faktoren des Gerinnungssystems im tiefgefrorenen Frischplasma während der Lagerung bei–20 °C und–40 °C. Infusionstherapie 11: 46–50

    CAS  Google Scholar 

  99. Koerner K, Stampe D, Kubanek B (1981) Das tiefgefrorene Frischplasma in der Blutkomponententherapie: Herstellung–Qualitätskontrolle–Indikation. Infusionstherapie 8: 253–258

    CAS  Google Scholar 

  100. Kreuz W, Auerswald G, Bruckmann C, Zieger B, Linde R, Funk M, Auberger K, Sutor AH, Rasshofer R, Roggendorf M (1992) Prevention of hepatitis C virus infection in children with haemophilia A and B and von Willebrand’s disease. Thromb Haemostas 67: 184 (letter)

    Google Scholar 

  101. Krijnen HW (1966) Herstellung, Eigenschaften und Verwendung von Plasmaproteinen. Monatskurse Ärztl Fortbildg 16: 131–134

    Google Scholar 

  102. Kurachi K, Davie EW (1982) Isolation and characterization of a cDNA coding for human factor IX. Proc Natl Acad Sci USA 79: 6461–6464

    PubMed  CAS  Google Scholar 

  103. Kurachi K (1991) Recombinant antihemophilie factors. In: Goldstein I (ed) Biotechnology of blood. Butterworth-Heinemann, Boston London Oxford, pp 177–195

    Google Scholar 

  104. Langner K-D, Bröker M, Zettlmeissl G (1990) Molecular biology of proteins involved in blood coagulation. Behring Inst Mitt 86: 146–169

    PubMed  CAS  Google Scholar 

  105. Lachmann PJ, Hughes-Jones NC (1984) Initiation of Complement activation. Springer Semin Immunopathol 7: 143–162

    PubMed  CAS  Google Scholar 

  106. Laurell CB (1960) Metall-binding plasma proteins and cation transport. In: Putnam FW (ed) The plasma proteins, vol I. Academic Press, New York London, pp 349–378

    Google Scholar 

  107. Laurell CB, Pierce J, Persson U, Thulin E (1975) Purification of a,-antitrypsin from plasma trough thiol-disulfide interchange. Eur J Biochem 57: 107–113

    PubMed  CAS  Google Scholar 

  108. Lechner K, Koller V, Pabinger I, Niessner HJ, Korniger CJ, Knapp WJ, Deutsch E (1985) Improvement of immunological status of hemophiliacs upon treatment with heat inactivated highly purified factor VIII concentrate. Thromb Haemost 54: 207

    Google Scholar 

  109. Liebman HA, Limentani SA, Furie BC, Furie B (1985) Immunoaffinity purification of factor IX (Christmas factor) by using conformation-specific antibodies directed against the factor IX-metal complex. Proc Nail Acad Sci USA 82: 3879–3883

    CAS  Google Scholar 

  110. Limentani SA, Roth DA, Furie BC, Furie B (1993) Recombinant blood clotting proteins for hemophilia therapy. Sem Thromb Hemost 19: 62–72

    CAS  Google Scholar 

  111. Lockridge O, La Du BN (1978) Comparison of atypical and usual human serum cholinesterase. Purification, number of active sites, substrate affinity and turnover number. J Biol Chem 253: 361–366

    PubMed  CAS  Google Scholar 

  112. Löbermann H, Lottspeich F, Bode W, Huber R (1982) Interaction of human-a proteinase inhibitor with chymotrypsinogen A and crystallization of a proteolytically modified a,-proteinase inhibitor. Hoppe Seyler’s Z Physiol Chem 363: 1377–1388

    PubMed  Google Scholar 

  113. Lo Grippo GA, Hartmann FW (1958) Chemical and combined methods for plasma sterilization. Bibl Haematol 7: 225–230

    Google Scholar 

  114. Mannucci PM, Zanetti AR, Colombo M (1988) Prospective study of hepatitis after factor VIII concentrate exposed to hot vapour. Br J Haematol 68: 427–430

    PubMed  CAS  Google Scholar 

  115. Mannucci PM, Schimpf K, Brettler DB, Ciavarelli N, Colombi M, Haschke F, Lechner K, Lusher J, Weissbach G and the International Study Group (1990) Low risk for hepatitis in haemophiliacs given a high-purity, pasteurized factor VIII concentrate. Ann Intern Med 113: 27–32

    PubMed  CAS  Google Scholar 

  116. Mannucci PM, Schimpf K, Abe T, Aledort LM, Anderle K, Brettler DB, Hilgartner MW, Kernoff PBA, Kunschak M, 139. McMillan CW, Preston FE, Rivard GE and the International Study Group (1992) Low risk of viral infection after administration of vapour heated factor VIII concentrates. Transfusion 32: 134–138

    Google Scholar 

  117. Mannucci PM (1993) Modern treatment of hemophila: From the shadows to the light. Thromb Haemostas 70: 17–23

    Google Scholar 

  118. McPherson A jr (1976) The growth and preliminary investigation of proteine and nucleic acid crystals for X-Ray diffraction analysis. Meth Biochem Anal 23: 249–345

    Google Scholar 

  119. McPherson A jr (1976) Crystallization of proteins from polyethylene glycol. J Biol Chem 251: 6300–6303

    PubMed  CAS  Google Scholar 

  120. Mellanby J (1905) Globulin. J Physiol (London) 33: 338–373

    Google Scholar 

  121. Ménaché D (1975) Factor IX Concentrates. Thrombos Diathes Haemorrh 33: 600–605

    Google Scholar 

  122. Miller-Andersson M, Borg H, Andersson LO (1974) Purification of Antithrombin III by Affinity Chromatography. Thromb Res 5: 439–452

    Google Scholar 

  123. Mösseler J, Schimpf K, Auerswald G, Bayer H, Schneider J, Hunsmann G (1985) Inability of pasteurised factor VIII preparations to induce antibodies to HTLV-II after long-term 145. treatment. Lancet i/8437: 1111

    Google Scholar 

  124. Mohr H, Lambrecht B, Knuever-Hopf J (1992) Virus inactivated single-donor fresh plasma preparations. Infusionstherapie 19: 79–83

    Google Scholar 

  125. Mosesson MW, Umfleet RA (1970) The coldinsoluble Globulin of human plasma. Purification, primary characterization, and relationship to fibrinogen and other cold-insoluble fraction components. j Biol Chem 245: 5728–5736

    Google Scholar 

  126. Mueller UW, Potter JM (1981) Purification and characterization of human Transcortin. Biochem J 197: 645–653

    Google Scholar 

  127. Müller-Eberhard U, English EC (1967) Purification and partial characterization of human hemopexin. J Lab Clin Med 70: 619–626

    PubMed  Google Scholar 

  128. Nees S (1974) Theoretical and practical aspects of high resolution preparative gel electrophoresis using a continuous elution system. In: Allen RC, Maurer HR (eds) Electrophoresis and isoelectric focusing in polyacrylamide gel. De Gruyter, Berlin, pp 189–199

    Google Scholar 

  129. Nilsson T, Wiman B (1982) Purification and Characterization of Human Cl-Esterase Inhibitor. Biochim Biophys Acta 705: 151. 271–276

    PubMed  CAS  Google Scholar 

  130. Nitschmann H, Kistler P, Lergier W (1954) Vereinfachtes Verfahren zur Gewinnung von humanem Albumin und Gamma-Globulin aus Blutplasma mittels Alkoholfällung. Helv Chim Acta 37: 866–876

    Google Scholar 

  131. Nitschmann H, Rickli E, Kistler P (1959) Über den Einfluß der Polyphosphate auf die Löslichkeit einiger Plasmaproteine und die Möglichkeit der Plasma-Fraktionierung mit Polyphosphat. Helv Chim Acta XLII: 2198–2211

    Google Scholar 

  132. Nitschmann H, Rickli E, Kistler P (1960) Fractionation of human plasma with polyphosphate. Vox Sang 5: 232–252

    PubMed  CAS  Google Scholar 

  133. Noyer M, Dwulet FE, Hao YL, Putnam FW (1980) Purification and characterization of undegraded human ceruloplasmin. Analyt Biochem 102: 450–458

    PubMed  CAS  Google Scholar 

  134. Oncley JL, Melin M, Richert DA, Cameron JW, Gross PM jr (1949) The Separation of the Antibodies, Isoagglutinins, Prothrobmin, Plasminogen and ß; Lipoprotein into Subfractions of Human Plasma. J Am Chem Soc 71: 541–550

    Google Scholar 

  135. Osborne JC jr, Brewer B jr (1977) The plasma lipoproteins. 157. In: Anfinsen CH, Edsall JT. Richards FM (eds) Adv Prot Chem 31: 253–337

    Google Scholar 

  136. lOstergaard K (1960) Herstellung von Plasmaprodukten fürdie therapeutische Anwendung. Dansk Tideskr Farm 34: 213–217

    Google Scholar 

  137. Pangborn MK, Müller-Eberhard HJ (1984) The alternative 159. pathway of complement. Springer Semin Immunopathol 7: 163–192

    Google Scholar 

  138. Pâques E (1980) Purification and partial characterization of the third component of the complement system from porcine serum (C3) and of a crystallizable degradation product of the fourth component of the complement system from human serum (C4). Hoppe Seyler’s Z Physiol Chem 361: 445–456

    Google Scholar 

  139. Pastewka JV, Ness AT, Peacock AC (1975) Hemoglobin binding by isolated polymeric proteins from human haptoglobin types 2–1 and 2–2: some suggested polymer subunit compositions. Biochim Biophys Acta 386: 530–537

    Google Scholar 

  140. Patrick CC, Virella G (1978) Isolation of normal human IgG 3. Identical molecular weight for normal and monoclonal gamma-3 chains. Immunochemistry 15: 137–139

    Google Scholar 

  141. Pennell RB (1960) Fractionation and Isolation of Purified Components by Precipitation Methods. In: Putnam FW (ed) The plasma proteins, vol I. Academic Press, New York London, pp 9–50

    Google Scholar 

  142. Pepper DS, Prowse C (1977) Chromatography of human pro-thrombin complex on dextran sulphate agarose. Thromb Res 11: 687–692

    PubMed  CAS  Google Scholar 

  143. Peterson EA, Sober HA (1956) Chromatography of proteins. I. Cellulose ion-exchange adsorbents. J Am Chem Soc 78: 751–755

    CAS  Google Scholar 

  144. Pflugshaupt R, Kurt G (1983) FPA Content — a Criterion of quality for plasma as factor VIII source. Vox Sang 45: 224–232

    PubMed  CAS  Google Scholar 

  145. Pillemer L, Hutchinson MC (1945) The determination of the albumin and globulin contents of human serum by methanol precipitation J Biol Chem 158: 299–301

    Google Scholar 

  146. Pillemer L, Blum L, Lepow JH, Ross OA, Todd EW, Ward-law AC (1954) The properdin system and immunity. I. Demonstration and isolation of a new serum protein, proper-din, and its role in immune phenomena. Science 120: 279–285

    Google Scholar 

  147. Poison A (1953) Multi-membrane electrodecantation and its application to isolation and purification of proteins and viruses. Biochem Biophys Acta 11: 315–325

    Google Scholar 

  148. Polsen A, Ruiz-Bravo C (1972) Fractionation of plasma with polyethylene glycol. Vox Sang 23: 107–118

    Google Scholar 

  149. Polsen A, Potgieter GM, Largier JF, Mears GEF, Joubert FG (1964) The fractionation of protein mixtures by linear poly- mers of high molecular weight. Biochim Biophys Acta 82: 463–475

    Google Scholar 

  150. Pool JG, Hershgold EJ, Pappenhagen AR (1984) High poten- cy antihaemophilic factor concentrate prepared from cryoglobulin precipitate. Nature (London) 203: 312

    Google Scholar 

  151. Porath J, Flodin P (1959) Gel filtration: A method for desalting and group separation. Nature (London) 183: 1657–1659

    CAS  Google Scholar 

  152. Porath J, Carlsson J, Olsson I, Belfrage G (1975) Metal chelate affinity chromatography, a new approach to protein fractionation. Nature (London) 258: 598–599

    CAS  Google Scholar 

  153. Prince AM, Stephan W, Dichtelmüller H et al. (1985) Inactivation of the Hutchinson strain of non-A, non-B hepatitis virus by combined use ß-propriolactone and ultraviolet irradiation. J Med Virol 16: 119–125

    PubMed  CAS  Google Scholar 

  154. Putnam FW (1977) Immunoglobulins I. Structure. In: Putnam FW (ed) The plasma proteins. vol III. Academic Press. New York San Francisco London, pp 1–153

    Google Scholar 

  155. Quazi MH, Mukherjee G, Javidi K, Pala A, Diczfalusy E (1974) Preparation of highly purified human chorionic gonadotrophin by isoelectric focusing. Eur J Biochem 47: 219–223

    Google Scholar 

  156. Radcliffe R, Heinze R (1978) Isolation of plasminogen activator from human plasma by chromatography on lysine-sepharose. Arch Biochem Biophys 189: 185–194

    PubMed  CAS  Google Scholar 

  157. Radola BJ (1974) Isoelectric focusing in layers of granulated gels II. Preparative isoelectric focusing. Biochim Biophys Acta 386: 181–195

    Google Scholar 

  158. Rock GA, Gruickshank WH, Tackaberry ES, Palmer DS (1979) Improved Yields of Factor VIII from Heparinized Plasma. Vox Sang 36: 294–300

    PubMed  CAS  Google Scholar 

  159. Sarver N, Ricca GA, Link J et al. (1987) Stable expression of recombinant factor VIII molecules using a bovine papillomavirus vector. DNA 6: 553–564

    PubMed  CAS  Google Scholar 

  160. Schimpf K, Zimmermann K (1980) Hepatitishäufigkeit, serologische Befunde und Leberhistologie nach Therapie schwerer Hämorrhagischer Diathesen mit Gerinnungsfaktorenkonzentraten. In: Schimpf K (Hrsg) Fibrinogen, Fibrin und Fibrinkleber. Schattauer, Stuttgart New York, S 229–308

    Google Scholar 

  161. Schimpf K, Mannucci PM, Kreuz W, Brackmann HH, Auerwald G, Ciavarella N, Moesseler J, De Rosa V, Kraus MD, Brueckman CH, Mancuso G, Mittler V, Haschke F, Morfini M (1987) Absence of hepatitis after treatment with a pasteurized factor VIII. N Engl J Med 316: 918–922

    PubMed  CAS  Google Scholar 

  162. Schmid J (1951) Die Blutgerinnung in Theorie und Praxis. Maudrich, Wien

    Google Scholar 

  163. Schmid K, Bürgi W (1961) Preparation and properties of the human plasma Ba-a, glycoprotein. Biochim Biophys Acta 47: 440–453

    Google Scholar 

  164. Schultze HE, Heremans JF (1966) Molecular Biology of Human Proteins, vol I. Elsevier, Amsterdam London New York

    Google Scholar 

  165. Schultze HE, Matheka HD (1954) Methoden und Ergebnisse der Plasmaprotein-Fraktionierung. Behringwerk Mitt 28: 962

    Google Scholar 

  166. Schultze HE, Schönenberger M, Matheka HD (1952) Zur Kenntnis der Gamma-Globuline und antitoxischen Immunglobuline. Behringwerk Mitt 26: 21–57

    Google Scholar 

  167. Schultze HE, Göllner I, Heide K, Schönenberger M, Schwick HG (1955) Zur Kenntnis der a-Globuline des menschlichen Normalserums. Z Naturforsch 10b: 463–473

    Google Scholar 

  168. Schultze HE, Heide K, Müller H (1957) Über Transferrin/Siderophilin. Behringwerk Mitt 32: 1–24

    Google Scholar 

  169. Schultze HE, Heide K, Haupt H (1962) a,-Antitrypsin aus Humanserum. Klin Wochenschr 40: 427–429

    Google Scholar 

  170. Schultze HE, Heide K, Haupt H (1962) Die mit Perchlorsäure nicht fällbaren Proteine des Humanserums. Clin Chim Acta 7: 854–868

    CAS  Google Scholar 

  171. Schultze HE, Haupt H, Heide K, Möschlin G, Schmidtberger R, Schwick HG (1962) Untersuchungen über Gamma-Makroglobuline des menschlichen Serums. Z Naturforsch 17b: 313–322

    Google Scholar 

  172. Schultze HE, Heimburger N, Heide K, Haupt H, Störiko K, Schwick HG (1963) Preparation and Characterization of a; Trypsin Inhibitor and a,-Plasmin Inhibitor of Human Serum. Proc 9th Congr Eur Soc Haematol Lisbon. Karger, Basel New York, pp 1315–1320

    Google Scholar 

  173. Schulman S, Lindgren AC, Petrini P, Allander T (1992) Transmission of hepatitis C with pasteurized Factor VIII. Lancet 2: 305–306 (letter)

    Google Scholar 

  174. Schwick HG, Haupt H (1980) Chemie und Funktion der Human-Plasmaproteine. Angew Chem 92: 83–95

    CAS  Google Scholar 

  175. Schwick HG, Haupt H (1984) Human plasma proteins of unknown function. In: Putnam FW (ed) The plasma proteins, vol IV. Academic Press, New York San Francisco London, pp 167–220

    Google Scholar 

  176. Schwick HG, Fischer J, Geiger H (1970) Human IgA- and IgM-globulins for clinical use. Proc mmth Int Congr Permanent Sect Microbiol Soc, Milan 1968, Proc Immunobiol Standard, Karger, Basel München New York, vol 4, pp 8691

    Google Scholar 

  177. Scott JD, Fothergill JE (1982) A general method for affinity purification of complement component C3b using factor HSepharose. Biochem J 205: 575–580

    PubMed  CAS  Google Scholar 

  178. Shuster L (1971) Preparative acrylamid gel electrophoresis: Continuous and disc techniques. In: Jacoby WB (ed) Methods in enzymology, vol 22. Academic Press, New York, pp 412–433

    Google Scholar 

  179. Sluyterman LAAE, Elgersma 0 (1978) Chromatofocusing; isoelectric focusing in ion exchange columns. I. General principles. J Chromatogr 150: 17–30

    CAS  Google Scholar 

  180. Smit JDG (1979) Reflections on protein crystallization. J Chim Phys Phys Chim Biol 76: 805–810

    CAS  Google Scholar 

  181. Smith LC, Pownall HJ, Gotto AM jr (1978) The plasma Lipoproteins: Structure and metabolism. Annu Rev Biochem 47: 751–777

    Google Scholar 

  182. Song MK, Adham NF, Rinderknecht H (1975) Large scale purification of a,-macroglobulin from human plasma. Biochem Med 14: 162–169

    PubMed  CAS  Google Scholar 

  183. Steinbuch M (1962) Les techniques d’isolement de l’haptoglobine. Nouv Rev Franc Hémat 2: 448

    PubMed  CAS  Google Scholar 

  184. Steinbuch M (1972) Precipitation methods in plasmaprotein fractionation. Vox Sang 23: 92–106

    PubMed  CAS  Google Scholar 

  185. Steinbuch M, Audran R (1965) Technique de purification des immuno-globulines. Transfusion 8: 141–163

    PubMed  CAS  Google Scholar 

  186. Steinbuch M, Audran R (1969) The isolation of IgG from mammalian sera with the aid of caprylic acid. Arch Biochem Biophys 134: 279–284

    PubMed  CAS  Google Scholar 

  187. Steinbuch M, Quentin M (1958) Preparation of Coeruloplasmin. Nature (London) 183: 323

    Google Scholar 

  188. Steinbuch M, Audran R, Pejaudier L (1970) Isolement d’immunoglobulines y, et y,, des plasma de chèvre de mouton et de b0000of. C R Soc Biol 164: 296–301

    CAS  Google Scholar 

  189. Stemberger A, Hörmann H (1976) Affinity chromatography on immobilized fibrinogen and fibrin monomer. II The Behavior of cold insoluble globulin. Hoppe Seyler’s Z Physiol Chem 357: 1003–1005.

    PubMed  CAS  Google Scholar 

  190. Stenflo J, Fernlund P, Egan W, Roepstorff P (1974) Vitamin K dependent modifications of glutamic acid residues in pro-thrombin. Proc Natl Acad Sci USA 71: 2730–2733

    PubMed  CAS  Google Scholar 

  191. Stephan W (1971) Hepatitis-free and stable human serum for intravenous therapy. Vox Sang 20: 442–457

    Google Scholar 

  192. Strop P, Borväk J, Kasicka V, Prusik Z, Morävek L (1981) Isolation of human hemopexin by bioaffinity chromatography on haeme-sepharose. J Chromatogr 214: 317–325

    Google Scholar 

  193. Surgenor DM, Pennell RB, Alameri E, Batchelor WH, Brown RK, Hunter MJ, Mannick VL (1960) Preparation and properties of serum and plasma proteins, XXXV. A System of protein fractionation using zink complexes. Vox Sang 5: 272–296

    CAS  Google Scholar 

  194. Tabor E, Murano G, Snoy P, Gerety RJ (1981) Inactivation of hepatitis B virus by heat in antithrombin III stabilized with citrate. Thromb Res 22: 233–238

    PubMed  CAS  Google Scholar 

  195. Taylor JF (1953) The Isolation of Proteins. In: Neurath H, Bailey K (eds) The proteins, vol I, part A. Academic Press, New York, pp 1–85

    Google Scholar 

  196. Thorell L, Blombäck B (1984) Purification of the Factor VIII Complex. Thromb Res 35: 431–450

    PubMed  CAS  Google Scholar 

  197. Toole JJ, Knopf JL, Wozney JM, Sultzman LA, Buecker JL, Pittman DD, Kaufman RJ, Brown E, Shoemaker C, Orr EC, Amphlett GW, Forster WB, Coe ML, Knutson GJ, Fass DN, Hewick RM (1984) Molecular cloning of a cDNA encoding human antihaemophilic factor. Nature (London) 312: 342–347

    Google Scholar 

  198. Travis J, Bowen J, Tewksbury D, Johnson D, Pannell R (1976) Isolation of albumin from whole human plasma and fractionation of the albumin-depleted plasma. Biochem J 157: 301–306

    PubMed  CAS  Google Scholar 

  199. Turba F, Enenkel AJ (1950) Elektrophorese von Proteinen in Filterpapier. Naturwissenschaften 37: 93

    CAS  Google Scholar 

  200. Turkovä J (1978) Affinity chromatography. Exemples of the use of affinity chromatography, vol 12, chap 11. J Chromatogr Lib, Elesvier, Amsterdam Oxford New York, pp 245–363

    Google Scholar 

  201. Vahlquist A, Nilsson S, Peterson PA (1971) Isolation of the human retinol binding protein by affinity chromatography. Eur J Biochem 20: 160–168

    PubMed  CAS  Google Scholar 

  202. Vehar GA, Keyt B, Eaton D, Rodriguez H, O’Brien DP (1984) Structure of human factor VIII. Nature (London) 312: 337–342

    Google Scholar 

  203. Volanakis JE, Clements WL, Schrohenloher RE (1978) C-reactive Protein: Purification by affinity chromatography and physicochemical characterization. J Immunol Meth 23: 285–295

    CAS  Google Scholar 

  204. Vuento M, Vaheri A (1978) Dissociation of Fibronectin from gelatinagarose by amino compounds. Biochem J 175: 333–336

    Google Scholar 

  205. Wichman A, Andersson LO (1974) Purification of human serum albumin by affinity chromatographie. Biochim Biophys Acta 372: 218–224

    PubMed  CAS  Google Scholar 

  206. Wickerhauser M (1976) Preparation of antihemophilic factor from indated plasma. Transfusion 16: 345–350

    Google Scholar 

  207. Wickerhauser M, Mercer JE, Eckenrode JW (1978) Development of Large-Scale Fractionation Methods. Vox Sang 35: 18–31

    PubMed  CAS  Google Scholar 

  208. Wickerhauser M,, Williams C, Mercer J (1979) Development of Large Scale Fractionation Methods: Preparation of Anti-thrombin III Concentrate. Vox Sang 36: 281–293

    PubMed  CAS  Google Scholar 

  209. Wieland T, Goldmann H, Kern W, Schultze HE, Matheka HD (1953) Versuche zur Fraktionierung von Proteingemischen mit Polyacrylsäuren. Makromol Chem 10: 136–146

    CAS  Google Scholar 

  210. Wiman B (1980) Human az antiplasmin. Meth Enzymol 80: 395–408

    Google Scholar 

  211. Wood WI, Capon DJ, Simonsen CC et al. (1984) Expression of active human factor VIII from recombinant DNA clones. Nature (London) 312: 330–337

    CAS  Google Scholar 

  212. Zettlmeissl G, Ragg H, Karges HE (1987) Expression of biologically active human antithrombin III in chinese hamster ovary cells. Biotechnology 5: 720–725

    CAS  Google Scholar 

  213. Zettlmeissl G, Karges HE (1989) Recombinant human factor XIII a: expression in mammalian cells and characterization. Thromb Haemostas 62: 346

    Google Scholar 

  214. Zimmerman TS (1988) Purification of factor VIII by monoclonal antibody affinity chromatography. Semin Haematol 25 [Supp1I]: 25–26

    CAS  Google Scholar 

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Heimburger, N., Haupt, H. (1996). Plasmafraktionierung. In: Mueller-Eckhardt, C. (eds) Transfusionsmedizin. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-10599-3_16

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