Literatur
Åkeson, A., G. Ehrenstein, G. Hevesy, andH. Theorell, Life Span of Myoglobin. Arch. Biochem. Biophys.91, 310–318 (1960).
Åkeson, A. andH. Theorell, On the Microheterogeneity of Horse Myoglobin. Arch. Biochem. Biophys.91, 319–325 (1960).
Åstrand, I., P. O. Åstrand, E. H. Christensen, andR. Hedman, Myohemoglobin as an Oxygen-Store in Man. Acta phys. Scand.48, 454–460 (1960).
Awad, E., L. Cameron, andL. Kotite, Chromatographic Separation of Hemoglobin and Myoglobin on „Sephadex” gel. Nature198, 1201–1202 (1963).
Benoit, F. L., G. B. Theil, andR. H. Watten, Foetal Myoglobin in the Urine of an Adult. Nature199, 387 (1963).
Berenbaum, M. C., C. A. Birch, andJ. D. Moreland, Paroxysmal Myoglobinuria. Lancet268, 892–896 (1955).
Berman, M. C. andJ. E. Keuck, Separation of Myoglobin and Hemoglobin on a Column of Dextran Gel. J. clin. Path.16, 385 (1963).
Bernofsky, C., J. B. Fox jr., andB. S. Schweigert Biochemistry of Myoglobin. 4. The Effects of low Dosage Gamma Irradiation on Beef Myoglobin. Arch. Biochem. Biophys.80, 9–21 (1959).
Betke, K. undW. Savelsberg, Stufenphotometrische Haemoglobinbestimmung mittels Cyanhaemiglobin. Biochem. Z.320, 431–439 (1950).
Betke, K., Der menschliche rote Blutfarbstoff bei Fetus und reifem Organismus (Berlin-Göttingen-Heidelberg 1954).
Betke, K., Diagnose und klinische Bedeutung der Haemoglobinanomalien. Internist1, 236–241 (1960).
Besnak, M., The Light Absorption of Sheep Hemoglobin and Myoglobin Compounds in the Soret-Region. Acta chem. Scand.2, 333–342 (1948).
Bingold, K., Über Ursachen und Symptome bei Haemolyse und Haemoglobinurie. Z. Klin. Med.126, 233–263 (1934).
Biörck, G., Myoglobin. Its Properties and Occurance in Man. Acta cardiol.3, 223–234 (1948).
Biörck, G., On Myoglobin and its Occurrence in Man. Acta med. Scand., Suppl.226, 133, 1–216 (1949).
Biörck, G., On Myoglobin and its Occurrence in Man (Stockholm 1949).
Blumgart, H. L., D. R. Gilligan, andM. J. Schlesinger, The Degree of myocardial Fibrosis in normal and pathologic Hearts as determined chemically by the Collagen Content. Trans. Ass. Amer. Physicians55, 313 (1940).
Boardmann, N. K. andG. S. Adair, Isolation of two Myoglobins from Horse Heart Extracts and the Determination of the Molecular Weight of the Main Component. Nature177, 1078–1079 (1956).
Bowen, W. J., Alkali Decomposition of Myoglobin. Fed. Proc.7, 11 (1948).
Bowen, W. J., Notes on Myoglobin Preparation and Iron Content. J. Biol. Chem.176, 747–751 (1948).
Bowen, W. J., The Absorption Spectra and Extinction Coefficients of Myoglobin. J. Biol. Chem.179, 235–245 (1949).
Bowen, W. J. andH. J. Eads, Effects of 18000 Feet Simulated Altitude on the Myoglobin Content of Dogs. Amer. J. Physiol.159, 77–82 (1949).
Bowen, W. J. andW. E. Poel, The Effects of Anoxia upon Myoglobin Concentration. Federation Proc.7, 11 (1948).
Bredauer, C., Pathologische Befunde bei Verschüttungen im Kriege. Inaug. Diss. (München 1920).
Bywaters, E. G. L. andJ. K. Stead, Thrombosis of the Femoral Artery with Myohemoglinuria and low Serum Potassium Concentration. Clin. Sci.5, 195–204 (1945).
Camus, J. andP. Pagniez, Hypohaemoglobine musculaire. Compt. rend. Soc. biol.56, 644–646 (1904).
Camus, J. andP. Pagniez, Hypohaemoglobin cardiaque. Compt. rend. Soc. biol.56, 773–775 (1904).
Clark, R. T. jr.,D. Criscuolo, andC. K. Coulson, Effects of 20 000 feet simulated Altitude on Myoglobin Content of Animals with and without Exercise. Fed. Proc.11, 25 (1952).
Colpa-Boonstra, J. P. andK. Minnaert, Myoglobin in Heart-Muscle Preparation and the Effect of Nitrite Treatment. Biochim. Biophys. Acta33, 527–534 (1959).
Crandall, M. W. andD. L. Drabkin, Cytochrome C in regenerating Rat Liver and its Relation to other Pigments. J. biol. chem.166, 653–668 (1946).
Crumpton, M. J., The immunological Activity of chymotryptic Peptides of Sperm-Whale Myoglobin. Biochem. J.91, 4c-6c (1964).
Dautrevaux, M. andS. Bernard, Études sur la myoglobine V. — Comparaison de la composition en acides aminés de quelques myoglobines d'espèces animales différentes. Bull. Soc. Chim. biol.44, 965–969 (1962).
Deutsch, K., Electron Microscope Examination of Myoglobin. Nature199, 180–181 (1963).
Drabkin, D. L., Crystallographic and optical Properties of human Hemoglobin. Amer. J. med. Sci.209, 268–270 (1945).
Drabkin, D. L., Crystalline human Hemoglobin and Myoglobin. Standardisation of the Hemoglobins and Denaturation Studies. Fed. Proc.4, 88 (1945).
Drabkin, D. L., The Distribution of the Chromoproteins, Hemoglobin, Myoglobin and Cytochrome C in the Tissues of different Species and the Relationship of the total Content of each Chromoprotein to Body Mass. J. Biol. Chem.182, 317–333 (1950).
de Duve, C., Spectrophotometric Method for the simultaneous Determination of Myoglobin and Hemoglobin in Extracts of human Muscle. Acta chem. Scand.2, 264–289 (1948).
Edmundson, A. B., Cleavage of Sperm-Whale Myoglobin with Cyanogen Bromide. Nature198, 354–359 (1963).
Fahlgren, H., R. Hed, andC. Lundmark, Myonecrosis and Myoglobinuria in Alcohol and Barbiturate Intoxication. Acta Med. Scand.158, 405–412 (1957).
Frankenthal, L., Über Verschüttungen. Virch. Arch.22, 332–345 (1916).
Gscheidlen, R., Bemerkungen zu der Welcher'schen Methode der Blutbestimmung und der Blutmenge einiger Säugetiere. Pflügers Arch.7, 530–548 (1873).
Günther, H., Über den Muskelfarbstoff. Virch. Arch.230, 146–178 (1921).
Havemann, R., F. Jung undB. v. Issekutz, Die Bestimmung von Methaemoglobin im Blute mit dem lichtelektrischen Kolorimeter. Biochem. Z.301, 116–124 (1939).
Hinsberg, K. undK. Lang, Medizinische Chemie. 3. Aufl. (München-Berlin-Wien 1957).
Hurtado, A., A. Rotta, C. Merino, andJ. Pons, Studies of Myohemoglobin at high Altitudes. Amer. J. Med. Sci.194, 708–713 (1937).
Ingram, D. J. E. andJ. C. Kendrew, Orientation of the Haem Group in Myoglobin and its Relation to the Polypeptide Chain Direction. Nature178, 905–906 (1956).
Jansen, H. H., Über den Bindegewebsgehalt des Herzmuskels. Verh. Dtsch. Ges. Path.46, 262–265 (1962).
Jonxis, H. H. P. andS. K. Wadman, A Fetal Form of Myoglobin. Nature169, 884–886 (1952).
Keilin, D., Nature of the Haem-Binding Groups in native and denatured Hemoglobin and Myoglobin. Nature187, 365–371 (1960).
Keilin, D., Precautions in the Use of Ferri- or Ferrocyanide for the Study of Hemoproteins. Nature190, 717–718 (1961).
Keilin, D. andE. F. Hartree, Effect of Drying upon the Absorption Spectra of Hemoglobin and its Derivatives. Nature170, 161–162 (1952).
Kendrew, J. C., Structure and Function in Myoglobin and other Proteins. Fed. Proc.18, 740–751 (1959).
Kendrew, J. C., Myoglobin and the Structure of Proteins. Sci.139, 1259–1266 (1963).
Kendrew, J. C., G. Bodo, H. M. Dintzis, R. G. Parrish, H. Wyckoff, andD. C. Phillips, A three-dimensional Model of the Myoglobin Molecule obtained by X-ray Analysis. Nature181, 662–666 (1958).
Kendrew, J. C., R. G. Parrish, J. R. Marrack, andE. S. Orland, The Species Specificity of Myoglobin. Nature174, 946–949 (1954).
Kiese, M. andH. Kaeske, Verbindungen des Muskelhämoglobins. Biochem. Z.312, 121–149 (1942).
Kiss, A. undW. Reinhart, Über den Nachweis des Myoglobins im Serum und im Harn nach Herzinfarkt. Weiner klin. Wschr.68, 154–155, (1956).
Knieriem, H. J., Über den Bindegewebsgehalt des Herzmuskels des Menschen. Arch. Kreislaufforschg.44, 231–259 (1964).
Kölliker, A., Mikroskopische Anatomie II,1 (Leipzig 1850).
de Langen, C. D., Myoglobin and Myoglobinuria. Acta Med. Scand.124, 213–226 (1946).
Lawrie, R. A., Crystalline Forms of Myoglobin from Horse Heart. Nature167, 802–804 (1951).
Lehmann, K. B., Untersuchungen über den Myoglobingehalt der Muskeln. Z. Biol.45, 324–345 (1904).
Lemberg, R. andJ. W. Legge, Hematin Compounds and Bile Pigments (New York-London 1949).
Levin, O., Electron microscopic Investigations of the Subunit of Hemoglobin and the Myoglobin Molecule J. molecular Biol.6, 158–163 (1963).
Lewis, U. H., Acid Cleavage of Heme Proteins. J. biol. chem.206, 109–120 (1954).
Lewis, U. H. andB. S. Schweigert, Biochemistry of Myoglobin. 3. Homogeneity Studies with cristalline Beef Myoglobin. J. Biol. Chem.214, 647–655 (1955).
Luginbuhl, W. H., A Method of Crystallization of Human Myoglobin. Proc. Soc. Exper. Biol. Med.105, 504–505 (1960).
Mann, H. B. undD. R. Whitney, ref. bei:Lienert, G. A., Verteilungsfreie Methoden in der Biostatistik, Anton Hain, Meisenheim am Glan, 1962, und beiSiegel, S., Nonparametric Statistics for the behavioral Sciences (New York 1956).
Mäsiar, P., Analogies and Differences between Human and Horse Myoglobin. Nature195, 507–508 (1962).
de Mello Mattos, C. M., R. Poche, H. W. Rembarz undK. Stoepel, Über das Verhältnis Mitochondrien: Myofibrillen in den Herzmuskelzellen der Ratte bei Druckhypertrophie des Herzens. Beitr. path. Anat. (im Druck).
Millikan, G. A., The Role of Muscle Hemoglobin. J. Physiol.87, 38p-39p (1936).
Minami, S., Über Nierenveränderungen nach Verschüttung. Virch. Arch.245, 247–267 (1923).
Miyoshi, K., K. Saijo, Y. Kuryn, andY. Oshima, Abnormal Myoglobin ultraviolet Spectrum in Duchenne Type of progressive muscular Dystrophy. Science142, 490–491 (1963).
Morgan, V. E., Studies on Myoglobin. 1. The Solubility of Myoglobin in concentrated Ammonium Sulfate Solutions. J. biol. chem.112, 557–563 (1936).
Mörner, K. A. H., Beobachtungen über den Muskelfarbstoff. Nord. med. Arkiv.30, 1–8 (1897).
Müller, F., Die Bestimmung der Blutmenge. Hdb. biochem. Arb. meth.3, 748–764 (1910).
McMunn, C. A., Further Observations on Myohematin and the Histohematins. Phil. Trans. Roy. Soc. London177, 235–266 (1886).
Perkoff, G. T., D. M. Brown, andF. H. Tyler, The Isolation of Myoglobin in Progressive Muscular Dystrophy. J. Clin. Endocrinol.17, 1489–1492 (1957).
Perkoff, G. T., R. L. Hill, andF. H. Tyler, Abnormal Myoglobin Chromatography in Childhood Muscular Dystrophy. J. Clin. Invest.41, 1391 (1962).
Perkoff, G. T., H. C. Schwarz, andF. H. Tyler, Incorporation of Radioiron into Myoglobin in an in-vitro System. J. clin. Invest.38, 1599–1604 (1959).
Perkoff, G. T. andF. H. Tyler, Estimation and physical Properties of Myoglobin in various Species. Metabolism7, 751–759 (1958).
Pick, L., Zur pathologischen Anatomie der Verschüttungen. Ärztl. Sachverständigen Zeitung2 (1920).
Poche, R., Die submikroskopische Morphologie des Herzmuskesl unter pathologischen Bedingungen. Verh. III Europ. Kardiologenkongreß (Rom 1960) Pavo prior 99.
Poche, R. undD. Mönkemeier, Quantitative morphologische Untersuchungen über das Verhältnis Mitochondrien: Myofibrillen in den Herzmuskelzellen bei Hungeratrophie und im Winterschlaf. Virch. Arch. path. Anat.335, 271–281 (1962).
Poel, W. E., Effect of anoxic Anoxia on Myoglobin Concentration in striated Muscle. Amer. J. Physiol.156, 44–61 (1949).
Porath, J. andP. Flodin, Gel Filtration: A Method for Desalting and Group Separation. Nature183, 1657–1659 (1959).
Poulik, M. O., Starch Gel Electrophoresis in a Discontinuous System of Buffers. Nature180, 1477–1479 (1957).
Rauen, M. H., Biochem. Taschenbuch I (Berlin 1964).
Recker, K., Über Gewebsmessungen, insbesondere Bestimmungen der Gewebsrelationen mit dem Integrationstisch (Leitz). Frankf. Z. Path.61, 137–148 (49/50).
Roche, J., Y. Derrien etH. Vieil, Recherches sur la composition et la spécificité des myoglobines (hémoglobines musculaires) de divers mammiféres. Bull. Soc. Chim. Biol.24, 1016–1026 (1942).
Rossi-Fanelli, A., Mioglobina umana cristallizzata. — III) Prime ricerche sulla costituzione chimica. Bol. Soc. Ital. Biol. Sper.23, 852–854 (1947).
Rossi-Fanelli, A., Crystalline human Myoglobin: Some physicochemical properties and chemical composition. Science108, 15–16 (1948).
Rossi-Fanelli, A., Chemical Composition of human Myoglobin. In: Hemoglobin, edit.F. J. W. Roughton andJ. C. Kendrew. S. 115–124 (London 1949).
Rossi-Fanelli, A. etE. Antonini, Sulla presenca di piu'mioglobine nei muscoli e nella mioglobina cristallizzata dei pesci. Bol. Soc. ital. biol. sper.32, 1156–1158 (1956).
Rossi-Fanelli, A. andE. Antonini, Heterogeneity of Human Myoglobin. Arch. Biochem.56, 587–590 (1956).
Rossi-Fanelli, A. andE. Antonini, Reversible splitting of human Myoglobin. Physicochemical Properties and Oxygen Equilibrium of reconstituted Proto- and Deuteromyoglobin. Arch. Biochem. Biophys.72, 243–246 (1957).
Rossi-Fanelli, A. andE. Antonini, Studies on the Oxygen and Carbonmonoxide Equilibria of human Myoglobin. Arch. Biochem. Biophys.77, 478–492 (1958).
Rossi-Fanelli, A., E. Antonini, andA. Caputo, Hemoglobin and Myoglobin. Advances Protein. Chem.19, 73–222 (1964).
Rossi-Fanelli, A., E. Antonini, andR. Guiffrè, Oxygen Equilibrium of Myoglobin from Thunnus Thynnus. Nature186, 896–897 (1960).
Rossi-Fanelli, A., D. Cavallini, andC. de Marco, Fetal Myoglobin. I. The Crystallization of human and Cow's Myoglobin extracted by the Heart and fetal Muscles. Arch. Biochem. Biophys.50, 496–502 (1954).
Rumen, N. M., Isolation of five Myoglobins from Seal (Phoca vitulina). Acta. chem. Scand.13, 1542–1546 (1959).
Schenk, J. H., J. L. Hall, andH. H. King, Spectrophotometric Characteristics of Hemoglobin. J. Biol. Chem.105, 741–752 (1934).
Schmid, K., Untersuchungen über das Wal-Myoglobin. Helv. Chim. Acta32, 105–114 (1949).
Schmid, K., Electrophoretic Properties and Analysis of Whale Myoglobin. Nature163, 481–482 (1949).
Schneiderman, L. J., Myoglobin in the human Fetus. Nature194, 191–192 (1962).
Schoenmackers, J., Vergleichende quantitative Untersuchungen über den Faserbestand des Herzens bei Herz- und Herzklappenfehlern sowie Hochdruck. Virch. Arch.331, 3–22 (1958).
Scouloudi, H., The Myoglobin Molecule. Nature183, 372–376 (1959).
Shikama, K., Chromatography of Oxy- and Met-Myoglobin on Diethylaminoethyl Cellulose Columns. Sci. Rep. Tòhoku Univ. Ser. IV, 30, 1–9 (1964).
Singer, K., B. Angelopoulos, andB. Ramot, Studies on human Myoglobin. I. Myoglobin in Sickle Cell Disease. Blood10, 979–986 (1955).
Singer, K., B. Angelopoulos, andB. Ramot, Studies on human Myoglobin. II. Fetal Myoglobin: Its Identification and its Replacement by Adult Myoglobin during Infancy. Blood10, 987–998 (1955).
Smith, M. H. andQ. H. Gibson, The Preparation and some Properties of Myoglobin containing Meso- and Deutero-Haem. Biochem. J.73, 101–106 (1959).
Smithies, O., Zone Electrophoresis in Starch Gels: Group Variations in the Serum Protein of normal human Adults. Biochem. J.61, 629–641 (1955).
Stegemann, H., Mikrobestimmung von Hydroxyprolin mit Chloramin-T and p-Dimethylaminobenzaldehyd. Beitr. path. Anat.311, 41–45 (1958).
Stich, W., Das Myorenale Syndrom. Regensb. Jahrb. für ärztl. Fortbild.6, 1 (1957/58).
Svedberg, T., Über die Ergebnisse der Ultrazentrifugierung und Diffusion für die Eiweißchemie. Kolloid-Z.85, 119–128 (1938).
Szent-Györgyi, A. G., in:G. H. Bourne, Structure and Function of Muscle, Vol. III (New York 1960).
Tappan, D. V. andB. Reynafarje, Tissue Pigment Manifestations of Adaptation to high Altitudes. Amer. J. Physiol.190, 99–103 (1957).
Theorell, H., Kristallinisches Myoglobin. I. Kristallisieren und Reinigung des Myoglobins, sowie vorläufige Mitteilung über sein Molekulargewicht. Biochem. Z.252, 1–7 (1932).
Theorell, H., Kristallinisches Myoglobin. III. Die absolute Licht-Absorption von Oxy-, CO-, Meta- und reduziertem Myoglobin. Biochem. Z.268, 55–63 (1934).
Theorell, H., Kristallinisches Myoglobin. IV. Mitteilung. Myoglobin im Gleichgewicht mit Sauerstoff und Kohlenoxyd. Biochem. Z.268, 64–72 (1934).
Theorell, H., Kristallinisches Myoglobin. V. Mitteilung. Die Sauerstoffbindungskurve des Myoglobins. Biochem. Z.268, 73–82 (1934).
Theorell, H. andA. Åkeson, Reversible Splitting of a homogeneous Horse Myoglobin. Ann. Acad. Scient. Fennicae60, 303–308 (1955) series A II.
Theorell, H. andC. de Duve, Crystalline Human Myoglobin from Heart-Muscle and Urine. Arch. Biochem.12, 113–124 (1947).
Theorell, H. andA. Ehrenberg, Spectrophotometric, magnetic and titrimetric Studies on the heme-linked Groups in Myoglobin. Acta chem. Scand.5, 823–848 (1951).
Tristram, G. R., The Amino Acid Composition of the Hemoglobins of the Blood and Muscle of the Horse. In: Hemoglobin, Barcroft Memorial Volume, edit. F. J. W. Roughton and J. C. Kendrew, p. 109–113, (London 1949).
Urnes, P. J., K. Imahori, andP. Doty, The optical rotatory Dispersion of right-handed alpha-Helices in Sperm-Whale Myoglobin. Proc. nat. Acad. Sci. U.S.A.47, 1635–1641 (1961).
Vanotti, A., The Adaptation of the Cell to Effort, Altitude and to pathological Oxygen Deficiency. Schweiz. med. Wschr.76, 899–903 (1946).
Vanotti, A., zitiert nachBelloni, L., Porphyries and Myoporphyries. Helvet. med. acta14, 3–21 (1947).
Vaughan, E. andN. Pace, Myoglobin Content of Rats at Sea Level and chronically exposed to Hypoxia.
Walters, C. L. andA. M. McTaylor, Differentiation of Myoglobins and Hemoglobins. Nature198, 996–997 (1963).
Watson, R. H., Some Observations on the Estimation of Muscle Hemoglobin. Bioch. J.29, 2114–2121 (1935).
Whipple, G. H., The Hemoglobin of Striated Muscle. Amer. J. Physiol.76, 693–707 (1926).
Whipple, G. H., The Hemoglobin of Striated Muscle. Amer. J. Physiol.76, 707–714 (1926).
Whipple, G. H. andW. W. Woodruff, Muscle Hemoglobin in human Autopsy Material. Amer. J. Pathol.4, 75–86 (1928).
Whorton, C. M., P. C. Hudgins, andJ. J. Conners, Abnormal spectrophotometric absorption Spectrums of Myoglobin in two Forms of Progressive Muscular Dystrophy. New Engl. J. Med.265, 1242–1245 (1961).
Wittenberg, J. B., Myoglobin-facilitated Diffusion of Oxygen. J. general Phys. Part II,491, 57–74 (1965).
Wollenberger, A., Die Mitochondrien im hypertrophen und insuffizienten Herzen. In: Wollheim und Schneider, Herzinsuffizienz, Haemodynamik und Stoffwechsel 202–221 (Stuttgart 1964).
Wollenberger, A., G. Raabe, B. Kleitke undW. Schulze, Über den Einfluß chronischer Herzüberbelastung auf Struktur und Funktion der Mitochondrien des Herzmuskels. Monatsber. Dtsch. Akad. Wiss. Berlin3, 597–600 (1961).
Wollenberger, A. undW. Schulze, Über das Volumenverhältnis von Mitochondrien zu Myofibrillen im chronisch überbelasteten, hypertrophierten Herzen. Naturwiss.49, 161–162 (1962).
Zollinger, H. U., Anurie bei Chromoproteinurie (Stuttgart 1952).
Author information
Authors and Affiliations
Additional information
Mit 8 Abbildungen in 10 Einzeldarstellungen und 16 Tabellen
Rights and permissions
About this article
Cite this article
Blessing, M.H. Über den Myoglobingehalt des Herzmuskels des Menschen. Archiv für Kreislaufforschung 52, 236–278 (1967). https://doi.org/10.1007/BF02119973
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF02119973