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Matrix models

Essential tools for microscopic cytochemical research

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Summary

An overview is given of the preparation and use of model systems for cytochemistry, dealing with quantitative as well as qualitative aspects.

Descriptions are given of the various possibilities to prepare cytochemical matrix models, ranging from macroscopic and microscopic films, to models with more cell-like dimensions as agarose beads, artificial cells and erythrocyte ghosts.

Such models allow the study of a large variety of cytochemical processes. Their potentialities are demonstrated in a number of specific applications, comprising: the study of the influence of fixation on cellular processes, reaction specificity and reaction kinetics, quality of reagents and biochemical calibration in cytochemical staining; factors influencing localization of the specific endproduct in enzyme cytochemistry; immunocytochemistry and hybridocytochemistry.

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References

  • Ahsmann WBAM, Duijn P van (1968) Amino acid cellulose films as models for histochemical protein reactions. Histochemie 12:285–288

    Google Scholar 

  • Andrä J, Dujin P van (1985) Quantitative aspects of cytochemical methods for acetyl-cholinesterase studied with a cytochemical model system. Histochemistry 83:443–449

    Google Scholar 

  • Axén R, Ernbäck S (1971) Chemical fixation of enzymes to cyanogen halide activated polysaccharide carriers. Eur J Biochem 18:351–360

    Google Scholar 

  • Axén R, Porath J (1966) Chemical coupling of enzymes to crosslinked dextran (‘Sephadex’). Nature 210:367–369

    Google Scholar 

  • Barbotin JN, Thomas D (1974) Electron microscopic and kinetic studies dealing with an artificial enzyme membrane. Application to a cytochemical model with the horseradish peroxidase 3,3′-diaminobenzidine system. J Histochem Cytochem 22:1048–1059

    Google Scholar 

  • Barnett RJ, Seligman AM (1954) Histochemical demonstration of sulphydryl and disulfide groups of protein. J Natl Cancer Inst 14:769–804

    Google Scholar 

  • Bauman JGJ, Wiegant JCAG, Duijn P van (1981) Cytochemical hybridization with fluorochrome-labeled RNA. I. Development of a method using nucleic acids bound to agarose beads as a model. J Histochem Cytochem 29:227–237

    Google Scholar 

  • Bauman JGJ, Wiegant JCAG, Duijn P van (1983) The development, using Poly(Hg-U) in a model system, of a new hybrid method to visualize cytochemical hybridization in fluorescence microscopy. J Histochem Cytochem 31:571–578

    Google Scholar 

  • Bauman JGJ, Ploeg M van der, Duijn P van (1984) Fluorescent hybridocytochemical procedures: DNA. RNA hybridization in situ. In: Chayen J, Bitensky L (eds) Investigative microtechniques in medicine and biology. Marcel Dekker, New York Basel, pp 41–87

    Google Scholar 

  • Blakesley RW, Boezi JA (1977) A new staining technique for proteins in polyacrylamide gels using Coomassie Brilliant Blue G250. Anal Biochem 82:580–582

    Google Scholar 

  • Broun G, Sélégny E, Avrameas S, Thomas D (1969) Enzymatically active membranes: some properties of cellophane membranes supporting cross-linked enzymes. Biochim Biophys Acta 185:260–262

    Google Scholar 

  • Chang TMS (1972) Artificial cells. CC Thomas, Springfield, IL

    Google Scholar 

  • Cohn NS (1973) A model system analysis of the parameters in histone staining. I. Alkaline Fast Green. Histochem J 5:529–545

    Google Scholar 

  • Cornelisse CJ, Duijn P van (1973) A new method for the investigation of the kinetics of the capture reaction in phosphatase cytochemistry. II. Theoretical and experimental study of phosphate diffusion from thin polyacrylamide films. J Histochem Cytochem 21:614–622

    Google Scholar 

  • Cornelisse CJ, Duijn P van (1974) A new method for the investigation of the capture reaction in phosphatase cytochemistry. III. Effects of the composition of the incubation medium on the trapping of phosphate ions in a model system. J Histochem Cytochem 22:110–119

    Google Scholar 

  • Cornelisse CJ, Hermens WTh, Tjok Joe M, Duijndam WAL, Duijn P van (1976) A theoretical study of concentration profiles of primary cytochemical enzyme reaction products in membranebound cell organelles and its application to lysosomal acid phosphatase. Histochem J 8:609–624

    Google Scholar 

  • Coujard R (1943) Essais sur la signification chimiques de quelques méthodes histologiques. Bull Histol Appl Physiol 20:161–173

    Google Scholar 

  • Coulet PR, Julliard JH, Gautheron BC (1974) A mild method of general use for covalent coupling of enzymes to chemically activated collagen films. Biotechnol Bioeng 16:1055–1068

    Google Scholar 

  • Dalen JPR van, Duijn P van (1971) Quantitative aspects of the ninhydrin-Schiff reaction on amino cellulose films and tissue sections. Histochemie 26:180–189

    Google Scholar 

  • Dalen JPR van, Haaijman JJ (1974) The determination of the molar absorbance coefficient of tetramethyl rhodamine isothiocyanate relative to fluorescein isothiocyanate. J Immunol Methods 5:103–106

    Google Scholar 

  • Dalen JPR van, Ahsmann WBAM, Duijn P van (1970) A method for the determination of the molar extinction coefficient of structure-linked chromophores. Histochem J 2:329–342

    Google Scholar 

  • Dalen JPR van, Knapp W, Ploem JS (1973) Microfluorometry on antigen-antibody interaction in immunofluorescence using antigens covalently bound to agarose beads. J Immunol Methods 2:383–392

    Google Scholar 

  • Davis BJ (1964) Disc electrophoresis. II. Method and application to human serum proteins. Ann NY Acad Sci 121:404–427

    Google Scholar 

  • Deelder AM, Snoijink JJ, Ploem JS (1975) Experimental optimization of the DASS system for immunodiagnosis of some helminth infections. Ann NY Acad Sci 177:119–136

    Google Scholar 

  • Deelder AM, Tanke HJ, Ploem JS (1978) Automated quantitative immunofluorescence using the aperture defined microvolume (ADM) method. In: Knapp W, Holubar K, Wick G (eds) Immunofluorescence and related staining techniques, Vienna Elsevier/North Holland Biomedical Press, Amsterdam, pp 31–44

    Google Scholar 

  • Deitch AD (1960) An improved Sakaguchi reaction for cytophotometric use. J Histochem Cytochem 8:325–326

    Google Scholar 

  • Deitch AD (1964) A method for the cytophotometric estimation of nucleic acids using methylene blue. J Histochem Cytochem 12:451–461

    Google Scholar 

  • Duijn P van (1957) Histochemistry of the DOPA factors. III. Inactivation experiments on the DOPA factors in neutrophilic and cosinophilic leucocytes and erythrocytes. Acta Physiol Pharmacol Neerl 5:428–444

    Google Scholar 

  • Duijn P van (1961) Acrolein-Schiff — a new staining method for proteins. J Histochem Cytochem 9:234–241

    Google Scholar 

  • Duijn P van (1974) Fundamental aspects of enzyme cytochemistry. In: Wisse E, Daems WTh, Molenaar I, Duijn P van (eds) Electron microscopy and cytochemistry. Proc 2nd Intern Symp Drienerlo, the Netherlands. North-Holland. Amsterdam, pp 3–23

    Google Scholar 

  • Duijn P van (1975) Carrier-bound model substances: a bridge between quantitative microscopical histochemistry and biochemistry. Acta Histochem (Suppl) 15:103–114

    Google Scholar 

  • Duijn P van (1976) Prospects for microscopical cytochemistry. A review. Histochem J 8:653–676

    Google Scholar 

  • Duijn P van (1978) Cytochemical markers in flow cytometry with special reference to specificity problems. In: Lutz D (ed) Pulsecytophotometry, vol III. European Press, Gent, pp 193–206

    Google Scholar 

  • Duijn P van, Ploeg M van der (1970) Potentialities of cellulose and polyacrylamide films as vehicles in quantitative cytochemical investigations on model substances. In: Wied GL, Bahr GF (eds) Introduction to quantitative cytochemistry, vol 2. Academic Press, New York London, pp 223–262

    Google Scholar 

  • Duijn P van, Ploeg M van der (1972) The use of cellulose and polyacrylamide films as vehicles of compounds for model studies in quantitative cytophotometry and for calibration of results in biochemical units. Acta Histochem (Suppl) 12:125–130

    Google Scholar 

  • Duijn P van, Ploeg M van der (1980) Microscopic cytochemistry as matrix chemistry. In: Trends in enzyme histochemistry and cytochemistry. Ciba Found Symp 73 (New series) Excerpta Medica Amsterdam, New York, pp 209–229

    Google Scholar 

  • Duijn P van, Pascoe E, Ploeg M van der (1967) Theoretical and experimental aspects of enzyme determination in a cytochemical model system of polyacrylamide films containing alkaline phosphatase. J Histochem Cytochem 15:631–645

    Google Scholar 

  • Duijndam WAL, Duijn P van (1975a) The interaction of apurinic acid aldehyde groups with pararosaniline in the Feulgen-Schiff and related staining procedures. Histochemistry 44:67–85

    Google Scholar 

  • Duijndam WAL, Duijn P van (1975b) The influence of chromatin compactness on the stoichiometry of the Feulgen-Schiff procedure studied in model films. I. Theoretical kinetics and experiments with films containing isolated deoxyribonucleic acid. J Histochem Cytochem 23:882–890

    Google Scholar 

  • Duijndam WAL, Duijn P van (1975c) The influence of chromatin compactness on the stoichiometry of the Feulgen-Schiff procedure studied in model films. II. Investigations on films containing condensed or swollen chicken erythrocyte nuclei. J Histochem Cytochem 23:891–900

    Google Scholar 

  • Duijndam WAL, Hermans J, Duijn P van (1973a) A new method to distinguish separate components in cytochemically stained macromolecules by analysis of the kinetics of the staining and destaining processes. J Histochem Cytochem 21:723–728

    Google Scholar 

  • Duijndam WAL, Hermans J, Duijn P van (1973b) Application of the method of kinetic analysis of staining and destaining processes to the complex formed between hydrolyzed deoxyribonucleoprotein and Schiff's reagent in model films. J Histochem Cytochem 21:729–736

    Google Scholar 

  • Fukuda M, Nakanishi K, Boehm N, Kimura J, Harada K, Fujita S (1979) Combined protein and DNA measurements by the ninhydrin-Schiff and Feulgen techniques. Histochemistry 63:35–45

    Google Scholar 

  • Gahrton G (1964) Microspectrophotometric quantitation of the periodic acid Schiff (PAS) reaction in human neutrophil leukocytes based on a model system of glycogen droplets. Exp Cell Res 34:488–506

    Google Scholar 

  • Gahrton G, Yataganas X (1976) Quantitative cytochemistry of glycogen in blood cells. Prog Histochem Cytochem 9

  • Gahrton G, Olsson I, Dalqvist A (1975) Determination of the glycogen content in single neutrophil leukocytes using a micro model of leukocyte glycogen. J Histochem Cytochem 23:59–64

    Google Scholar 

  • Geerts A, Roels F (1981) Quantitation of catalase activity by microspectrophotometry after diaminobenzidine staining. Histochemistry 72:357–367

    Google Scholar 

  • Gerritsen WJ, Verkley AJ, Zwaal RFA, Deenen LLM van (1978) Freeze-fracture appearance and disposition of band 3 protein from the human erythrocyte membrane in lipid vesicles. Eur J Biochem 85:255–261

    Google Scholar 

  • Goldman R, Lenhoff HM (1971) Glucose-6-phosphate dehydrogenase adsorbed on collodion membranes. Biochim Biophys Acta 242:514–518

    Google Scholar 

  • Goldman R, Silman MJ, Caplan SR, Kedem O, Katchalski E (1965) Papain membrane on a collodion matrix, preparation and enzymic behaviour. Science 150:758–760

    Google Scholar 

  • Goldstein E, Bartlema HC, Ploeg M van der, Duijn P van, Stap JGMM van der, Lippert W (1978) Effect of ozone on lysosomal enzymes of alveolar macrophages engaged in phagocytosis and killing of inhaled Staphylococcus aureus. J Infect Dis 138:299–311

    Google Scholar 

  • Goldstein DJ, Horobin RW (1974) Rate factors in staining by alcian blue. Histochem J 6:157–174

    Google Scholar 

  • Guilbault GG (1977) Enzyme electrodes and solid surface fluorescence methods. In: Mosbach K (ed) Methods in enzymology, vol 44:Immobilized enzymes. Academic Press, New York, pp 579–633

    Google Scholar 

  • Haaijman JJ (1977) Quantitative immunofluorescence microscopy. Methods and applications. Thesis, Leiden 1977

  • Haaijman JJ, Dalen JPR van (1974) Quantitation in immunofluorescence microscopy. A new standard for fluorescein and rhodamine emission measurements. J Immunol Methods 5:358–374

    Google Scholar 

  • Habeeb AFSA (1967) Preparation of enzymically active, waterinsoluble derivatives of trypsin. Arch Biochim Biophys 119:264–268

    Google Scholar 

  • Hand AR, Hassell JR (1976) Tissue fixation with diimido esters alternative to aldehyde. II. Cytochemical and biochemical studies of rat liver fixed with dimethyl suberimidate. J Histochem Cytochem 24:1000–1011

    Google Scholar 

  • Hardonk MJ, Duijn P van (1964a) Studies on the Feulgen reaction with histochemical model systems. J Histochem Cytochem 12:758–767

    Google Scholar 

  • Hardonk MJ, Duijn P van (1964b) Synthesis and properties of model systems, with their use in studying the Schiff reaction in histochemistry. J Histochem Cytochem 12:533–537

    Google Scholar 

  • Holt SJ, O'Sullivan DG (1958) Studies in enzyme cytochemistry. I. Principles of cytochemical staining methods. Proc R Soc 148 B: 495–505

    Google Scholar 

  • Hopman AHN, Wiegant JCAG, Duijn P van (1986) A new hybricocytochemical method based on mercurated nucleic acid probes and sulphydryl-hapten ligands. (Submitted)

  • Hopwood D (1969) Fixatives and fixation: a review. Histochem J 1:323–360

    Google Scholar 

  • Hopwood D (1985) Cell and tissue fixation, 1972–1982. Histochem J 17:389–442

    Google Scholar 

  • Hopwood D, Mellors AE (1973) An investigation of the chlorotriazine derivatives as fixatives for tissues. Histochem J 5:391–403

    Google Scholar 

  • Jong ASH de, Duijn P van (1980) The dynamics of calcium phosphate precipitation studied with a new polyacrylamide steady state matrix-model: Influence of pyrophosphate, collagen and chondroitin sulfate. Connect Tissue Res 7:73–79

    Google Scholar 

  • Jong ASH de, Ploeg M van der (1977) Chemical and histochemical latency of alkaline phosphatase in granules of neutrophilic leucocytes. J Histochem Cytochem 25:1184–1186

    Google Scholar 

  • Jong ASH de, Duijn P van, Daems WTh (1976) Cytochemical model systems for microsomal rat liver glucose-6-phosphatase. J Histochem Cytochem 24:643–651

    Google Scholar 

  • Jong ASH de, Hak TJ, Tjok Joe M, Duijn P van (1978a) Enzyme layers on glass as a new model for the quantitative study of capture reactions in cytochemistry, with special attention to acid phosphatase. Histochemistry 57:273–284

    Google Scholar 

  • Jong ASH de, Hak TJ, Duijn P van, Daems WTh (1978b) A new dynamic model system for the study of capture reactions for diffusable compounds in cytochemistry. I. Description of the model with special attention to phosphate capture in acid phosphatase cytochemistry. J Histochem Cytochem 26:331–339

    Google Scholar 

  • Jong ASH de, Hak TJ, Duijn P van, Daems WTh (1979a) A new dynamic model system for the study of capture reactions for diffusable compounds in cytochemistry. II. Effect of the composition of the incubation medium on the trapping of phosphate ions in acid phosphate cytochemistry. Histochem J 11:145–161

    Google Scholar 

  • Jong ASH de, Hak TJ, Duijn P van, Daems WTh (1979b) A new dynamic model system for the study of capture reactions for diffusable compounds in cytochemistry. III. Influence of the matrix composition on the lead phosphate precipitation process in acid phosphatase cytochemistry. Histochem J 11:163–171

    Google Scholar 

  • Julliard JH, Godinot C, Gautheron DC (1971) Some modifications of the kinetic properties of liver glutamate dehydrogenase (NAD(P)) covalently bound to a solid matrix of collagen. FEBS Lett 14:185–188

    Google Scholar 

  • Kay G, Crook EM (1967) Coupling of enzymes to cellulose using chloro-5-triazines. Nature 216:514–515

    Google Scholar 

  • Kay G, Killy MD (1970) The chemical attachment of chymotrypsine to water insoluble polymers using 2-amino-4,6-dichloro-s-triazine. Biochim Biophys Acta 198:276–285

    Google Scholar 

  • Kelly JW, Carlsson L (1963) Protein droplets, especially gelatin, hemoglobin and histone, as microscopic standards for quantitation of cytochemical reactions. Exp Cell Res 30:106–124

    Google Scholar 

  • Kopriwa BM (1966) A semiautomatic instrument for the radioautographic coating technique. J Histochem Cytochem 14:923–928

    Google Scholar 

  • Landing BH, Hall HE (1956) Selective demonstration of histidine. Stain Technol 31:533–537

    Google Scholar 

  • Leeman U, Ruch F (1972) Cytofluorometric determination of basic and total proteins with sulfaflavine. J Histochem Cytochem 20:659–671

    Google Scholar 

  • Lojda Z, Ploeg M van der, Duijn P van (1967) Phosphates of the naphthol series in the quantitative determination of alkaline and acid phosphatase activities “in situ” studied in polyacrylamide membrane model systems and by cytospectrophotometry. Histochemie 11:13–32

    Google Scholar 

  • Malpièce Y, Sharan M, Barbotin JN, Personne P, Thomas D (1980) A histochemical model dealing with an immobilized glucose oxidase-peroxidase system. The influence of diffusion limitations on histochemical results. J Histochem Cytochem 28:961–968

    Google Scholar 

  • Malpièce Y, Sharan M, Barbotin J, Personne P, Thomas D (1981) Kinetic, compouter and electron microscopic studies dealing with an artificial enzyme membrane. Theoretical and experimental evaluation of the cytochemical demonstration of acetyl cholinesterase. J Histochem Cytochem 29:633–643

    Google Scholar 

  • Mekuda E, Yamaizumi M, Uchida T, Okada Y (1978) Quantitative introduction of a given macromolecule into cells by fusion with erythrocyte ghosts using a fluorescence activated cells sorter. J Histochem Cytochem 26:1067–1073

    Google Scholar 

  • Micheel F, Ewers J (1949) Symthese von Verbindungen der Cellulose mit Eiweißstoffen. Makromol Chem 3:200–209

    Google Scholar 

  • Millar DA, Williams ED (1982) A step-wedge standard for the quantification of immunoperoxidase techniques. Histochem J 14:609–620

    Google Scholar 

  • Mitchell JP (1975) Combined staining of protein-bound sulphydryl groups and DNA in polyacrylamide model systems. Histochem J 7:283–290

    Google Scholar 

  • Mitchell JP (1977) Model studies of staining procedures for lysine and arginine residues. Histochemistry 52:151–157

    Google Scholar 

  • Mitchell JP, Ploeg M van der, Duijn P van (1981) Combined staining procedures for cytophotometry of protein and DNA: Feulgen-Naphthol Yellow S and Dinitrofluorobenzene-Feulgen. Histochemistry 73:211–223

    Google Scholar 

  • Mitz MA, Summaria LJ (1961) Synthesis of biologically active cellulose derivatives of enzymes. Nature 189:576–577

    Google Scholar 

  • Molin SD, Nygren H, Dolonius L (1978a) A new method for the study of glutaraldehyde induced crosslinking properties in proteins with special reference to the reaction with amino groups. J Histochem Cytochem 26:412–414

    Google Scholar 

  • Molin SD, Nygren H, Dolonius L, Hansson H (1978b) A kinetic study of the reaction between glutaraldehyde and horseradish peroxidase. J Histochem Cytochem 26:1053–1056

    Google Scholar 

  • Mosbach K (1977) (ed) Immobilized enzymes. Methods in Enzymology, vol 44. Academic Press, New York

    Google Scholar 

  • Mosbach R, Koch-Schmidt AC, Mosbach K (1977) Immobilization of enzymes to various acrylic copolymers. In: Mosbach K (ed) Methods in enzymology, vol 44: Immobilized enzymes. Academic Press, New York, pp 53–65

    Google Scholar 

  • Mulder MP, Duijn P van, Gloor HJ (1968) The replication organization of DNA in polytene chromosomes of Drosophila hydei. Genetica 39:385–428

    Google Scholar 

  • Mykoniatis MG (1985) Immobilization of native and denatured DNA on Sephadex G200. J Biochem Biophys Methods 10:321–328

    Google Scholar 

  • Nakae Y, Shono M (1984) Quantitative double-staining methods for tryptophyl and cysteinyl residues and proteins in model films. Histochem J 16:51–59

    Google Scholar 

  • Noorden CJF van, Tas J (1980) Quantitative aspects of the enzyme cytochemical demonstration of glucose-6-phosphate dehydrogenase with tetranitro BT studied in a model system of polyacrylamide films. Histochem J 12:669–685

    Google Scholar 

  • Noorden CJF van, Tas J (1981) Model film studies in enzyme histochemistry with special reference to glucose-6-phosphatase dehydrogenase. Histochem J 13:187–206

    Google Scholar 

  • Noorden CJF van, Tas J (1982) The role of exogenous electron carriers in NAD(P)-dependent dehydrogenase cytochemistry studies in vitro and with a model system of polyacrylamide films. J Histochem Cytochem 30:12–20

    Google Scholar 

  • Noorden CJF van, Tas J, Sanders JAH (1981) Quantitative aspects of the cytochemical demonstration of glucose-6-phosphate dehydrogenase with tetrazolium salts studied in a model system of polyacrylamide films. Acta Histochem (Suppl) 24:231–236

    Google Scholar 

  • Noorden CJF van, Tas J, Vogels IMC, Schepper GG de (1982) A new method for the enzyme cytochemical staining of individual cells with the use of a polyacrylamide carrier. Histochemistry 74:171–181

    Google Scholar 

  • Oud PS, Henderik JBJ, Huysmans ACLM, Pahlplatz MMM, Hermkens HG, Tas J, James J, Vooys GP (1984) The use of Light Green and Orange II as quantitative protein stains, and their combination with the Feulgen method for the simultaneous determination of protein and DNA. Histochemistry 80:49–57

    Google Scholar 

  • Papadimitriou JM, Duijn P van (1970a) Effects of fixation and substrate protection on the isoenzymes of aspartate aminotransferase studied in a quantitative cytochemical model system. J Cell Biol 47:71–83

    Google Scholar 

  • Papadimitriou JM, Duijn P van (1970b) The ultrastructural localization of the isoenzymes of aspartate amino transferase in murine tissues. J Cell Biol 47:84–98

    Google Scholar 

  • Partanen S, Bäck N (1979) Quantitative fluorescence histochemistry of combined formaldehyde-chloral-induced fluorescence of amino-terminal tryptophyl-peptide in model experiments and in the pars intermedia of the rat hypophysis. Histochemistry 61:291–300

    Google Scholar 

  • Persijn JP, Duijn P van (1961) Studies of the Feulgen reaction with the aid of DNA incorporated cellulose films. Histochemie 2:283–291

    Google Scholar 

  • Pette D, Wimmer M (1979) Kinetic microphotometric activity determination in enzyme containing gels and model studies with tissue sections. Histochemistry 64:11–22

    Google Scholar 

  • Pilwat G, Washausen P, Klein J, Zimmermann U (1980) Immobilization of human red blood cells. Z Naturforsch 35c:352–356

    Google Scholar 

  • Ploeg M van der, Duijn P van (1964) The influence of peroxidases on the DOPA-system. J R Microse Soc 83:405–414

    Google Scholar 

  • Ploeg M van der, Duijn P van (1966) Quantitative cytophotometric determination of glycogen in neutrophilic leucocytes. Proc R Microsc Soc 1:131

    Google Scholar 

  • Ploeg M van der, Duijn P van (1968) Cytophotometric determination of alkaline phosphatase activity of individual neutrophilic leukocytes with a biochemically calibrated model system. J Histochem Cytochem 16:693–706

    Google Scholar 

  • Ploeg M van der, Streefkerk JG, Daems WTh, Brederoo P (1974) Quantitative aspects of cytochemical peroxidase reactions with 3,3′-diamino-benzidine and 5,6-dihydroxy indole as substrates. In: Wisse E, Daems WTh, Molenaar I, Duijn P van (eds) Electron microscopy and cytochemistry. North-Holland, Amsterdam, 123–126

    Google Scholar 

  • Ploeg M van der, Broek K van der, Mitchell JP (1979) Dual wavelength seanning cytophotometry (BICOSCAN). Histochemistry 62:29–43

    Google Scholar 

  • Ploem JS (1975) General Introduction. In: “Fifth International Conference on Immunofluorescence and related staining techniques”. Ann NY Acad Sci 254: 4–20

  • Ploem JS (1980) Appropriate technology for the quantitative assessment of the final reaction product of histochemical techniques. In: Trends in enzyme histochemistry and cytochemistry. Ciba Found Symp 73 (new series) pp 275–303

  • Porath J, Axén R (1977) Immobilization of enzymes to agar, agarose, and Sephadex supports. In: Mosbach K (ed) Methods in enzymology, vol 44: Immobilized enzymes. Academic Press, New York, pp 19–45

    Google Scholar 

  • Porath J, Axén R, Ernbäck S (1967) Chemical coupling of proteins to agarose. Nature 215:1491–1492

    Google Scholar 

  • Prooijen-Knegt AC van, Redi CA, Ploeg M van der (1980) Quantitative aspects of the cytochemical Feulgen-DNA procedure studied on model films and cell nuclei. Histochemistry 69:1–17

    Google Scholar 

  • Prooijen-Knegt AC van, Hoek JFM van, Bauman JGJ, Duijn P van, Wool IG, Ploeg M van der (1982) In situ hybridization of DNA sequences in human metaphase chromosomes visualised by an indirect fluorescent immuno-cytochemical procedure. Exp Cell Res 141:397–407

    Google Scholar 

  • Prosperi E, Raap AK (1982) Short communications: Substrate protection during the fixation of β-glucuronidase: cytochemical model system studies. Histochem J 14:689–695

    Google Scholar 

  • Prosperi E, Raap AK, Ploeg M van der (1982) Histochemical model studies of enzyme activity after thermal damage. Histochemistry 75:387–397

    Google Scholar 

  • Raap AK (1983) Studies on the phenazine methosulphate-tetrazolium salt capture reaction in NAD(P)+-dependent dehydrogenase cytochemistry. III. The role of superoxide in tetrazolium reduction. Histochem J 15:977–986

    Google Scholar 

  • Raap AK, Duijn P van (1981) Enzyme-incorporated erythrocyte ghosts: a new model system for quantitative enzyme cytochemistry. J Histochem Cytochem 29:1418–1424

    Google Scholar 

  • Raap AK, Duijn P van (1983) Studies on the phenazine methosulphate-tetrazolium salt capture reaction in NAD(P)+-dependent dehydrogenase cytochemistry. II. A novel hypothesis for the model of action of PMS and a study of the properties of reduced PMS. Histochem J 15:881–893

    Google Scholar 

  • Raap AK, Hoof GRM van, Duijn P van (1983) Studies on the phenazine methosulphate-tetrazolium salt capture reaction in NAD(P)+-dependent dehydrogenase cytochemistry. I Localization artefacts caused by the escape of reduced co-enzyme during cytochemical reactions for NAD(P)+-dependent dehydrogenases. Histochem J 15:861–879

    Google Scholar 

  • Raap AK, Marijnen JGJ, Ploeg M van der (1984) Anti-DNA.RNA sera. Specificity tests and application in quantitative in situ hybridization. Histochemistry 81:517–520

    Google Scholar 

  • Rappay G, Duijn P van (1964) Aminoethylcellulose membranes as model for a quantitative cytochemical study of the ninhydrin-Schiff reaction. Abstr 2nd Intern Congr Histochem Cytochem, Frankfurt, Germany, Summary Repts, p. 188, Springer, Berlin

    Google Scholar 

  • Rigler R Jr (1966) Microfluorometric characterization of intracellular nucleic acids and nucleoproteins by acridine orange. Acta Physiol Scand (Suppl) 67:267

    Google Scholar 

  • Ritzén M (1966) Quantitative fluorescence microspectrophotometry of catecholamine-formaldehyde products. Model experiments. Exp Cell Res 44:505–529

    Google Scholar 

  • Ritzén M (1967) Quantitative fluorescence microspectrophotometry of catecholamine-formaldehyde products in models and in mast cells. Exp Cell Res 45:178–194

    Google Scholar 

  • Satterfield CN, Sherwood TK (1963) The role of diffusion in catalysis. Addison-Wesley, Redding, MA, pp 56–63

    Google Scholar 

  • Schipper J, Tilders FJH (1982) Quantification of formaldehyde induced fluorescence and its application in neurobiology. Brain Res Bull 9:169–181

    Google Scholar 

  • Schipper J, Tilders FJH (1983) A new technique for studying specificity of immunocytochemical procedures, specificity of serotonin immunostaining. J Histochem Cytochem 31:12–18

    Google Scholar 

  • Sélégny E, Avrameas S, Broun G, Thomas D (1968) Membranes à activité enzymatique. Synthèses de membranes à enzymes liées par covalence, characterisation de l'activité catalytique par diffusion-réaction. CR Acad Sci Ser C 266:1431

    Google Scholar 

  • Sernetz M, Puchinger H, Couwenbergs C, Ostwald M (1976) A new method for the evaluation of the reaction kinetics of immobilised enzymes investigated in single enzyme-sepharose beads by microfluorometry. Anal Biochem 72:24–37

    Google Scholar 

  • Singer M, Morrison PR (1948) The influence of pH, dye and salt concentration on the dye binding of modified and unmodified fibrin. J Biol Chem 175:133–145

    Google Scholar 

  • Squier CA, Hart JS, Churchland A (1976) Changes in red blood cell volume on fixation in glutaraldehyde solutions. Histochemistry 48:7–16

    Google Scholar 

  • Streefkerk JG, Ploeg M van der (1973) Quantitative aspects of cytochemical peroxidase peroxidase procedures investigated in a model system. J Histochem Cytochem 21:715–722

    Google Scholar 

  • Streefkerk JG, Ploeg M van der (1974) The effect of methanol on granulocyte and horseradish peroxidase quantitatively studied in a film model system. Histochemistry 40:105–111

    Google Scholar 

  • Streefkerk JG, Ploeg M van der, Kors N (1975a) Some aspects of immuno-histoperoxidase reactions in the agarose bead model system. Ann NY Acad Sci 254:212–222

    Google Scholar 

  • Streefkerk JG, Ploeg M van der, Duijn P van (1975b) Agarose beads as matrices for proteins in cytophotometric investigation of immunoperoxidase procedures. J Histochem Cytochem 23:243–250

    Google Scholar 

  • Tas J (1975) Histochemical conditions influencing metachromatic staining. A comparative study by means of a model system of polyacrylamide films. Histochem J 7:1–19

    Google Scholar 

  • Tas J (1977) The Alcian Blue and combined Alcian Blue-Safranin O staining of glycosaminoglycans studied in a model system and in mast cells. Histochem J 9:205–230

    Google Scholar 

  • Tas J, Roozemond RC (1973) Direct recording of metachromatic spectra in a model system of polyacrylamide films. Histochem J 5:425–436

    Google Scholar 

  • Tas J, Westerneng G (1981) Fundamental aspects of the interaction of propidium diiodide with nucleic acids studied in a model system of polyacrylamide films. J Histochem Cytochem 29:929–936

    Google Scholar 

  • Tas J, Oud P, James J (1974) The Naphtol Yellow S stain for proteins tested in a model system of polyacrylamide films and evaluated for practical use in histochemistry. Histochemistry 40:231–240

    Google Scholar 

  • Tas J, James J, Ploeg M van der (1978) Adaptation of the naphthol yellow S staining for objects with high protein content. Histochemistry 55:185–195

    Google Scholar 

  • Tas J, Frederiks WM, Frank JJ (1979a) A new approach to the staining of lipids with Sudan Black B: a study by means of polyacrylamide model films containing liposomes. Acta Histochem (Suppl) 21:123–129

    Google Scholar 

  • Tas J, Vries ACJ de, Berndsen RG (1979b) A method for the quantitative determination of protein incorporated in solubilizable polyacrylamide gels. Anal Biochem 100:264–270

    Google Scholar 

  • Tas J, Ploeg M van der, Mitchell JP, Cohn NS (1980) Protein staining methods in quantitative cytochemistry. J Microsc 117:295–311

    Google Scholar 

  • Tas J, Mendelsohn D, Noorden CJF van (1983) Cuprolinic Blue: a specific dye for single stranded RNA in the presence of magnesiumchloride. I. Fundamental aspects. Histochem J 15:801–814

    Google Scholar 

  • Thomas D, Broun G (1977) Artificial enzyme membranes. In: Mosbach K (ed) Methods in enzymology, vol 44: Immobilized enzymes. Academic Press, New York, pp 901–929

    Google Scholar 

  • Tilders FJH, Ploem JS, Smelik PG (1974) Quantitative microfluorimetric studies on formaldehyde-induced fluorescence of 5-hydroxy tryptamine in the pineal gland of the rat. J Histochem Cytochem 22:967–975

    Google Scholar 

  • Toepfer K (1975) Quantitative Untersuchungen der metachromatischen Reaktion von Mukopolysacchariden in Polyacrylamid Membranen nach der Van-Duijn-Methode. Acta Histochem (Suppl) 14:187–196

    Google Scholar 

  • Tonkelaar EM den, Duijn P van (1964) Photographic colorimetry as a quantitative cytochemical method. III. Determination of the absolute amount of DNA in cell nuclei. Histochemie 4:16–19

    Google Scholar 

  • Troyer H, Rosenquist TH (1975) Atomic absorption spectrophotometry applied to photographic densitometry. J Histochem Cytochem 23:941–944

    Google Scholar 

  • Tsuji S (1974) On the chemical basis of thiocholine methods for demonstration of acetylcholine esterase activities. Histochemistry 42:99–110

    Google Scholar 

  • Valnes K, Brandtzaeg P (1985) Retardation of immunofluorescence fading during microscopy. J Histochem Cytochem 33:755–761

    Google Scholar 

  • Vieth WR, Wang SS, Gilbert SG (1972) Urea hydrolysis on collagen-urease complex membrane. Biotechnol Bioeng Symp 3:285–297

    Google Scholar 

  • Wada A, Kishizaki A (1968) Chromatographic studies with immobilized polynucleotide in acrylamide gel matrix. Biochim Biophys Acta 166:29–39

    Google Scholar 

  • Weetall HH (1968) Covalent coupling methods for inorganic support materials. In: Mosbach K (ed) Methods in enzymology, vol 44: Immobilized enzymes. Academic Press, New York, pp 134–148

    Google Scholar 

  • Wenk H, Krug H, Fletcher AM (1973) Eine mikrospektrofotometriche Methode zur quantitativen Aktivitätsbestimmung von Acetyl-Cholinesterase an Gewebeschnitten. Acta Histochem 45:37–60

    Google Scholar 

  • Wilson RJH, Kay G, Lilly MD (1968) The preparation and kinetics of lactate dehydrogenase attached to water-insoluble particles and sheets. Biochem J 108:845–853

    Google Scholar 

  • Wittekind DH, Gehring T (1985) On the nature of Romanowsky-Giemsa staining and the Romanowsky-Giemsa effect. I. Model experiments on the specificity of Azure B-Eosin Y stain as compared with other thiazine dye-Eosine Y combinations. Histochem J 17:263–289

    Google Scholar 

  • Wolters GHJ, Pasma A, Konijnendijk W, Bouman PR (1979) Evaluation of the glyoxal-bis-(2-hydroxyanil)-method for staining of calcium in model gelatin films and pancreatic islands. Histochemistry 62:137–151

    Google Scholar 

  • Yamamoto N (1977) Application of metal labeled antibody method and a consideration of the fixatives suitable for immunohistochemical study. Acta Histochem Cytochem Jpn 10:246–252

    Google Scholar 

  • Yamamoto N, Yasuda K (1977) Use of a water soluble carbodiimide as a fixing reagent. Acta Histochem Cytochem Jpn 10:14–37

    Google Scholar 

  • Yokota S (1973) Assay of antihorseradish peroxidase antibody in an immunocytochemical model system of polyacrylamide gel films. J Histochem Cytochem 21:779–784

    Google Scholar 

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In honour of Prof. P. van Duijn

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van der Ploeg, M., Duijndam, W.A.L. Matrix models. Histochemistry 84, 283–300 (1986). https://doi.org/10.1007/BF00482953

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