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Volumn 1, Issue PA, 1983, Pages 469-516

Enzyme activity staining

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EID: 33747379226     PISSN: 01687972     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-444-42226-2.50031-1     Document Type: Chapter
Times cited : (534)

References (90)
  • 1
    • 49849124235 scopus 로고
    • Ascorbate oxidase isozymes
    • Anion, A., Markakis, P., Ascorbate oxidase isozymes. Phytochemistry 8 (1961), 997–998.
    • (1961) Phytochemistry , vol.8 , pp. 997-998
    • Anion, A.1    Markakis, P.2
  • 2
    • 2342489739 scopus 로고
    • The use of a diazonium salt for the determination of glutamic-oxalacetic transaminase in serum
    • Babson, A.L., Shapiro, P.O., Williams, P.A.R., Phillips, G.E., The use of a diazonium salt for the determination of glutamic-oxalacetic transaminase in serum. Clin. Chim. Acta 7 (1962), 199–205.
    • (1962) Clin. Chim. Acta , vol.7 , pp. 199-205
    • Babson, A.L.1    Shapiro, P.O.2    Williams, P.A.R.3    Phillips, G.E.4
  • 3
    • 0000839947 scopus 로고
    • Method for the detection of glutamine synthetase activity on starch gels
    • Barratt, D.H.P., Method for the detection of glutamine synthetase activity on starch gels. Plant Sci. Lett. 18 (1980), 249–255.
    • (1980) Plant Sci. Lett. , vol.18 , pp. 249-255
    • Barratt, D.H.P.1
  • 4
    • 70449178680 scopus 로고
    • Histochemical demonstration of protein-bound alpha-acylamido carboxyl groups
    • Barrnett, R.J., Seligman, A.M., Histochemical demonstration of protein-bound alpha-acylamido carboxyl groups. J. Biophys. Biochem. Cytol. 4 (1958), 169–176.
    • (1958) J. Biophys. Biochem. Cytol. , vol.4 , pp. 169-176
    • Barrnett, R.J.1    Seligman, A.M.2
  • 5
    • 33947440019 scopus 로고
    • Amylose and amylopectin content of starches determined by their iodine complex formation
    • Bates, F.L., French, D., Rundle, R.E., Amylose and amylopectin content of starches determined by their iodine complex formation. J. Am. Chem. Soc. 65 (1943), 142–148.
    • (1943) J. Am. Chem. Soc. , vol.65 , pp. 142-148
    • Bates, F.L.1    French, D.2    Rundle, R.E.3
  • 6
    • 0015153416 scopus 로고
    • Superoxide dismutase: improved assays and an assay applicable to acrylamide gels
    • Beauchamp, C., Fridovich, I., Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44 (1971), 276–287.
    • (1971) Anal. Biochem. , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 7
    • 0020076404 scopus 로고
    • Est-6, a further polymorphic esterase in the rat
    • Bender, K., Nagel, M., Gunther, E., Est-6, a further polymorphic esterase in the rat. Biochem. Genet. 20 (1982), 221–229.
    • (1982) Biochem. Genet. , vol.20 , pp. 221-229
    • Bender, K.1    Nagel, M.2    Gunther, E.3
  • 8
    • 0345179388 scopus 로고
    • The demonstration of thiol groups in certain tissues by means of a new colored sulfhydryl reagent
    • Bennett, H.S., The demonstration of thiol groups in certain tissues by means of a new colored sulfhydryl reagent. Anat. Rec. 110 (1951), 231–248.
    • (1951) Anat. Rec. , vol.110 , pp. 231-248
    • Bennett, H.S.1
  • 9
    • 33947453415 scopus 로고
    • Spectrophotometric study of the reaction of protein sulfhydryl groups with organic mercurials
    • Boyer, P.D., Spectrophotometric study of the reaction of protein sulfhydryl groups with organic mercurials. J. Am. Chem. Soc. 76 (1954), 4331–4337.
    • (1954) J. Am. Chem. Soc. , vol.76 , pp. 4331-4337
    • Boyer, P.D.1
  • 11
    • 0014218072 scopus 로고
    • A starch gel electrophoretic method for the study of diaphorase isozymes and preliminary results with sheep and human erythrocytes
    • Brewer, G.J., Eaton, J.W., Knutsen, C.S., Beck, C.C., A starch gel electrophoretic method for the study of diaphorase isozymes and preliminary results with sheep and human erythrocytes. Biochem. Biophys. Res. Commun. 29 (1967), 198–204.
    • (1967) Biochem. Biophys. Res. Commun. , vol.29 , pp. 198-204
    • Brewer, G.J.1    Eaton, J.W.2    Knutsen, C.S.3    Beck, C.C.4
  • 12
    • 0018234762 scopus 로고
    • Genetic variation in natural populations of wild barley (Hordeum spontaneum)
    • Brown, A.H.D., Nevo, E., Zohary, D., Dagan, O., Genetic variation in natural populations of wild barley (Hordeum spontaneum). Genetica 49 (1978), 97–108.
    • (1978) Genetica , vol.49 , pp. 97-108
    • Brown, A.H.D.1    Nevo, E.2    Zohary, D.3    Dagan, O.4
  • 13
    • 0009047222 scopus 로고
    • Purification and properties of carbonic anhydrase from Chlamydomonas reinhardii
    • Bundy, H.F., Cote, S., Purification and properties of carbonic anhydrase from Chlamydomonas reinhardii. Phytochemistry 19 (1980), 2531–2534.
    • (1980) Phytochemistry , vol.19 , pp. 2531-2534
    • Bundy, H.F.1    Cote, S.2
  • 14
  • 15
    • 0014030716 scopus 로고
    • Electrophoretic heterogeneity of mammalian galactose dehydrogenase
    • Cuatrecasas, P., Segal, S., Electrophoretic heterogeneity of mammalian galactose dehydrogenase. Science 154 (1966), 533–535.
    • (1966) Science , vol.154 , pp. 533-535
    • Cuatrecasas, P.1    Segal, S.2
  • 16
    • 0020057743 scopus 로고
    • Tissue-specific and substrate-specific detection of aldehyde and pyridoxal oxidase in larval and imaginal tissues of Drosophila melanogaster
    • Cypher, J.J., Tedesco, J.L., Courtright, J.B., Kumaran, A.K., Tissue-specific and substrate-specific detection of aldehyde and pyridoxal oxidase in larval and imaginal tissues of Drosophila melanogaster. Biochem. Genet. 20 (1982), 315–332.
    • (1982) Biochem. Genet. , vol.20 , pp. 315-332
    • Cypher, J.J.1    Tedesco, J.L.2    Courtright, J.B.3    Kumaran, A.K.4
  • 17
    • 0014019274 scopus 로고
    • Free aldehydic groups in collagen and other tissue components
    • Davis, R.P., Janis, R., Free aldehydic groups in collagen and other tissue components. Nature 210 (1966), 318–319.
    • (1966) Nature , vol.210 , pp. 318-319
    • Davis, R.P.1    Janis, R.2
  • 19
    • 0344705256 scopus 로고
    • Multiple forms of glutamic-oxalacetic transaminase in tissues
    • Decker, L.E., Rau, E.M., Multiple forms of glutamic-oxalacetic transaminase in tissues. Proc. Soc. Exp. Biol. Med. 112 (1963), 144–149.
    • (1963) Proc. Soc. Exp. Biol. Med. , vol.112 , pp. 144-149
    • Decker, L.E.1    Rau, E.M.2
  • 20
    • 0018069624 scopus 로고
    • Purification of blood carbonic anhydrase and specific detection of carbonic anhydrase isoenzymes on polyacrylamide gels with 5-dimethylaminonaphthalene-l-sulfonamide (DNSA)
    • Drescher, D.G., Purification of blood carbonic anhydrase and specific detection of carbonic anhydrase isoenzymes on polyacrylamide gels with 5-dimethylaminonaphthalene-l-sulfonamide (DNSA). Anal. Biochem. 90 (1978), 349–358.
    • (1978) Anal. Biochem. , vol.90 , pp. 349-358
    • Drescher, D.G.1
  • 21
    • 0014029063 scopus 로고
    • Hexokinase isozyme patterns of human erythrocytes and leucocytes
    • Eaton, G.M., Brewer, G.J., Tashian, R.E., Hexokinase isozyme patterns of human erythrocytes and leucocytes. Nature 212 (1966), 944–946.
    • (1966) Nature , vol.212 , pp. 944-946
    • Eaton, G.M.1    Brewer, G.J.2    Tashian, R.E.3
  • 22
    • 0008118250 scopus 로고
    • The detection of some naturally occurring flavanone compounds on paper chromatography
    • Eigen, E., Blitz, M., Gunsberg, E., The detection of some naturally occurring flavanone compounds on paper chromatography. Arch. Biochem. Biophys. 68 (1957), 501–502.
    • (1957) Arch. Biochem. Biophys. , vol.68 , pp. 501-502
    • Eigen, E.1    Blitz, M.2    Gunsberg, E.3
  • 23
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, G.L., Tissue sulfhydryl groups. Arch. Bioch. Biophys. 82 (1959), 70–77.
    • (1959) Arch. Bioch. Biophys. , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 24
    • 0014015348 scopus 로고
    • Genetically determined variation of adenylate kinase in man
    • Fildes, R.A., Harris, H., Genetically determined variation of adenylate kinase in man. Nature 209 (1966), 261–263.
    • (1966) Nature , vol.209 , pp. 261-263
    • Fildes, R.A.1    Harris, H.2
  • 25
    • 0000464402 scopus 로고
    • The use of starch electrophoresis in dehydrogenase studies
    • Colowick S.P. Kaplan N.O. Academic Press New York
    • Fine, I.H., Costello, L.A., The use of starch electrophoresis in dehydrogenase studies. Colowick, S.P., Kaplan, N.O., (eds.) Methods in Enzymology, VI, 1963, Academic Press, New York, 958–972.
    • (1963) Methods in Enzymology , vol.6 , pp. 958-972
    • Fine, I.H.1    Costello, L.A.2
  • 26
    • 0005941506 scopus 로고
    • A sensitive and non-inhibitory catalytic gel stain for urease
    • In Fifth International Symposyum on Chromatography and Electrophoresis in Brussels. Humphrey Science Publishers Inc. Ann Arbor
    • Fishbein, W.N. 1969. A sensitive and non-inhibitory catalytic gel stain for urease. In Fifth International Symposyum on Chromatography and Electrophoresis in Brussels. Humphrey Science Publishers Inc. Ann Arbor, pp. 238–241.
    • (1969) , pp. 238-241
    • Fishbein, W.N.1
  • 27
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske, C.H., Subbarow, Y., The colorimetric determination of phosphorus. J. Biol. Chem. 66 (1925), 375–400.
    • (1925) J. Biol. Chem. , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 28
    • 84979187519 scopus 로고
    • Amylase isozymes in germinating barley seeds
    • Frydenberg, O., Nielsen, G., Amylase isozymes in germinating barley seeds. Hereditas 54 (1966), 123–139.
    • (1966) Hereditas , vol.54 , pp. 123-139
    • Frydenberg, O.1    Nielsen, G.2
  • 29
    • 0343108891 scopus 로고
    • Formazans and tetrazolium salts
    • R.D. Lillie H.J. Conn's Williams and Wilkins Company Baltimore
    • Glenner, G.G., Formazans and tetrazolium salts. Lillie, R.D., Conn's, H.J., (eds.) Biological Stains, 1977, Williams and Wilkins Company, Baltimore, 225–235.
    • (1977) Biological Stains , pp. 225-235
    • Glenner, G.G.1
  • 30
    • 0013788124 scopus 로고
    • The cytochemical demonstration of lysosomal aryl sulfatase activity by light and electron microscopy
    • Goldfischer, S., The cytochemical demonstration of lysosomal aryl sulfatase activity by light and electron microscopy. J. Histochem. Cytochem. 13 (1965), 520–522.
    • (1965) J. Histochem. Cytochem. , vol.13 , pp. 520-522
    • Goldfischer, S.1
  • 31
    • 84960567744 scopus 로고
    • Microtechnical demonstration of phosphatase in tissue sections
    • Gomori, G., Microtechnical demonstration of phosphatase in tissue sections. Proc. Soc. Exp. Biol. Med. 42 (1939), 23–26.
    • (1939) Proc. Soc. Exp. Biol. Med. , vol.42 , pp. 23-26
    • Gomori, G.1
  • 32
    • 0001498672 scopus 로고
    • Distribution of acid phosphatase in the tissues under normal and under pathologic conditions
    • Gomori, G., Distribution of acid phosphatase in the tissues under normal and under pathologic conditions. Arch. Pathol. 32 (1941), 189–199.
    • (1941) Arch. Pathol. , vol.32 , pp. 189-199
    • Gomori, G.1
  • 33
    • 78651175275 scopus 로고
    • Cytochemical demonstration of peroxidase activity with 3-amino-9-ethylcarbazole
    • Graham, R.C., Lundholm, U., Karnovsky, M.J., Cytochemical demonstration of peroxidase activity with 3-amino-9-ethylcarbazole. J. Histochem. Cytochem. 13 (1964), 150–152.
    • (1964) J. Histochem. Cytochem. , vol.13 , pp. 150-152
    • Graham, R.C.1    Lundholm, U.2    Karnovsky, M.J.3
  • 34
    • 0000490682 scopus 로고
    • Electrophoretic profiles of cyanobacterial membrane polypeptides showing heme-dependent peroxidase activity
    • Guikema, J.A., Sherman, L.A., Electrophoretic profiles of cyanobacterial membrane polypeptides showing heme-dependent peroxidase activity. Biochim. Biophys. Acta 637 (1980), 189–201.
    • (1980) Biochim. Biophys. Acta , vol.637 , pp. 189-201
    • Guikema, J.A.1    Sherman, L.A.2
  • 35
    • 0000060578 scopus 로고
    • Fluorometric determination of lipase, acylase, alpha- and gamma-chymotrypsin and inhibitors of these enzymes
    • Guilbault, G.G., Kramer, D.N., Fluorometric determination of lipase, acylase, alpha- and gamma-chymotrypsin and inhibitors of these enzymes. Anal. Chem. 36 (1964), 409–412.
    • (1964) Anal. Chem. , vol.36 , pp. 409-412
    • Guilbault, G.G.1    Kramer, D.N.2
  • 36
    • 0038538387 scopus 로고
    • The oxidation-reduction enzymes of wheat. III. Isoenzymes of lipoxidase in wheat fractions and soybean
    • Guss, P.L., Richardson, T., Stahmann, H.A., The oxidation-reduction enzymes of wheat. III. Isoenzymes of lipoxidase in wheat fractions and soybean. Cereal Chem. 44 (1967), 607–610.
    • (1967) Cereal Chem. , vol.44 , pp. 607-610
    • Guss, P.L.1    Richardson, T.2    Stahmann, H.A.3
  • 39
    • 0010273348 scopus 로고
    • Organ specific multiple forms of glutamic dehydrogenase in Medicago sativa
    • Hartmann, T., Nagel, M., Ilert, H-I., Organ specific multiple forms of glutamic dehydrogenase in Medicago sativa. Planta 111 (1973), 119–128.
    • (1973) Planta , vol.111 , pp. 119-128
    • Hartmann, T.1    Nagel, M.2    Ilert, H.-I.3
  • 40
    • 0347599654 scopus 로고
    • The effect of menadione and phenazine methosulfate on the tetrazolium reduction system under histochemical conditions
    • Hashimoto, T., Kaluza, J.S., Burstone, M.S., The effect of menadione and phenazine methosulfate on the tetrazolium reduction system under histochemical conditions. J. Histochem. Cytochem. 12 (1964), 797–804.
    • (1964) J. Histochem. Cytochem. , vol.12 , pp. 797-804
    • Hashimoto, T.1    Kaluza, J.S.2    Burstone, M.S.3
  • 41
    • 36949064248 scopus 로고
    • Cytochemical localization of pyridine nucleotide-linked dehydrogenases
    • Hess, R., Scarpelli, D.G., Pearse, A.G.E., Cytochemical localization of pyridine nucleotide-linked dehydrogenases. Nature 181 (1958), 1531–1532.
    • (1958) Nature , vol.181 , pp. 1531-1532
    • Hess, R.1    Scarpelli, D.G.2    Pearse, A.G.E.3
  • 43
    • 0015763453 scopus 로고
    • A staining method for nitrate reductase on polyacrylamide gels after electrophoresis
    • Hucklesby, D.P., Hageman, R.H., A staining method for nitrate reductase on polyacrylamide gels after electrophoresis. Anal. Biochem. 56 (1973), 591–592.
    • (1973) Anal. Biochem. , vol.56 , pp. 591-592
    • Hucklesby, D.P.1    Hageman, R.H.2
  • 44
    • 85023326555 scopus 로고
    • Identification and translocation of carbohydrates in the cantaloupe (Cucumis melo var. reticulatus) plant and the fate of stachyose during fruit development
    • Ph. D. Thesis. University of California, Davis
    • Hughes, D.L. 1981. Identification and translocation of carbohydrates in the cantaloupe (Cucumis melo var. reticulatus) plant and the fate of stachyose during fruit development. Ph. D. Thesis. University of California, Davis.
    • (1981)
    • Hughes, D.L.1
  • 45
    • 0001362081 scopus 로고
    • Histochemical demonstration of enzymes separated by zone electrophoresis in starch gels
    • Hunter, R.L., Markert, C.L., Histochemical demonstration of enzymes separated by zone electrophoresis in starch gels. Science 125 (1957), 1294–1295.
    • (1957) Science , vol.125 , pp. 1294-1295
    • Hunter, R.L.1    Markert, C.L.2
  • 48
    • 0000393850 scopus 로고
    • Genetics of isozyme variants in barley
    • Kahler, A.L., Allard, R.W., Genetics of isozyme variants in barley. I. Esterases. Crop Sci. 10 (1970), 444–448.
    • (1970) I. Esterases. Crop Sci. , vol.10 , pp. 444-448
    • Kahler, A.L.1    Allard, R.W.2
  • 49
    • 0014338429 scopus 로고
    • Detection of multiple forms of proteolytic enzymes by starch gel electrophoresis
    • Kaminski, E., Bushuk, W., Detection of multiple forms of proteolytic enzymes by starch gel electrophoresis. Can. J. Biochem. 46 (1968), 1317–1320.
    • (1968) Can. J. Biochem. , vol.46 , pp. 1317-1320
    • Kaminski, E.1    Bushuk, W.2
  • 50
    • 0014480751 scopus 로고
    • Effect of sulfhydryl reagents on glucose determination by the glucose oxidase method
    • Kilburn, D.M., Taylor, P.M., Effect of sulfhydryl reagents on glucose determination by the glucose oxidase method. Anal. Biochem. 27 (1969), 555–558.
    • (1969) Anal. Biochem. , vol.27 , pp. 555-558
    • Kilburn, D.M.1    Taylor, P.M.2
  • 51
    • 0002435505 scopus 로고
    • The Distribution of Sulfur Compounds
    • T. Swain Academic Press London, New York
    • Kjaer, A., The Distribution of Sulfur Compounds. Swain, T., (eds.) Chemical Plant Taxonomy, 1963, Academic Press, London, New York, 453–473.
    • (1963) Chemical Plant Taxonomy , pp. 453-473
    • Kjaer, A.1
  • 52
    • 0001464749 scopus 로고
    • Colorimetric determination of succinic dehydrogenase by triphenyl tetrazolium chloride
    • Kun, E., Abood, L.G., Colorimetric determination of succinic dehydrogenase by triphenyl tetrazolium chloride. Science 109 (1949), 144–146.
    • (1949) Science , vol.109 , pp. 144-146
    • Kun, E.1    Abood, L.G.2
  • 53
    • 84907126062 scopus 로고
    • Histochemical demonstration of pyrophosphatase
    • Kurata, Y., Maeda, S., Histochemical demonstration of pyrophosphatase. Stain Technol. 31 (1956), 13–16.
    • (1956) Stain Technol. , vol.31 , pp. 13-16
    • Kurata, Y.1    Maeda, S.2
  • 54
    • 0003439655 scopus 로고
    • 9th. edition Williams and Wilkins Company Baltimore
    • Lillie, R.D., Conn's, H.J., (eds.) Biological Stains, 9th. edition, 1977, Williams and Wilkins Company, Baltimore, 613.
    • (1977) Biological Stains , pp. 613
    • Lillie, R.D.1    Conn's, H.J.2
  • 55
    • 0002394619 scopus 로고
    • A specific micromethod for the determination of acyl phosphates
    • Lipman, F., Tuttle, L.C., A specific micromethod for the determination of acyl phosphates. J. Biol. Chem. 159 (1945), 21–28.
    • (1945) J. Biol. Chem. , vol.159 , pp. 21-28
    • Lipman, F.1    Tuttle, L.C.2
  • 56
    • 0012466667 scopus 로고
    • Triphenytetrazolium chloride as a dye for vital tissues
    • Mattson, A.M., Jensen, C.O., Dutcher, R.A., Triphenytetrazolium chloride as a dye for vital tissues. Science 106 (1947), 294–295.
    • (1947) Science , vol.106 , pp. 294-295
    • Mattson, A.M.1    Jensen, C.O.2    Dutcher, R.A.3
  • 57
    • 0000535586 scopus 로고
    • Multiple forms of enzymes: tissue, ontogenic and species specific patterns
    • Markert, C.L., Moller, F., Multiple forms of enzymes: tissue, ontogenic and species specific patterns. Proc. Nat. Acad. Sci. USA 45 (1959), 753–763.
    • (1959) Proc. Nat. Acad. Sci. USA , vol.45 , pp. 753-763
    • Markert, C.L.1    Moller, F.2
  • 59
    • 0019154368 scopus 로고
    • Rare structural variants of human and murine uroporphyrinogen I synthase
    • Meisler, M.H., Carter, M.L.C., Rare structural variants of human and murine uroporphyrinogen I synthase. Proc. Nat. Acad. Sci. USA 77 (1980), 2848–2852.
    • (1980) Proc. Nat. Acad. Sci. USA , vol.77 , pp. 2848-2852
    • Meisler, M.H.1    Carter, M.L.C.2
  • 60
    • 0344766833 scopus 로고
    • A coupling histochemical azo dye test for alkaline phosphatase in the kidney
    • Menten, M.L., Junge, J., Green, M., A coupling histochemical azo dye test for alkaline phosphatase in the kidney. J. Biol. Chem. 153 (1944), 471–477.
    • (1944) J. Biol. Chem. , vol.153 , pp. 471-477
    • Menten, M.L.1    Junge, J.2    Green, M.3
  • 61
    • 0014832182 scopus 로고
    • Reactions of superoxide anion, catechols, and cytochrome c
    • Miller, R.W., Reactions of superoxide anion, catechols, and cytochrome c. Can. J. Biochem. 48 (1970), 935–939.
    • (1970) Can. J. Biochem. , vol.48 , pp. 935-939
    • Miller, R.W.1
  • 62
    • 33947550088 scopus 로고
    • The chemistry of formazans and tetrazolium salts
    • Nineham, A.W., The chemistry of formazans and tetrazolium salts. Chem. Rev. 55 (1955), 355–483.
    • (1955) Chem. Rev. , vol.55 , pp. 355-483
    • Nineham, A.W.1
  • 63
    • 0015168580 scopus 로고
    • Carbonic anhydrase: a new method of detection on polyacrylamide gels using low-temperature fluorescence
    • Patterson, B.D., Atkins, C.A., Graham, D., Wills, R.B.H., Carbonic anhydrase: a new method of detection on polyacrylamide gels using low-temperature fluorescence. Anal. Biochem. 44 (1971), 388–391.
    • (1971) Anal. Biochem. , vol.44 , pp. 388-391
    • Patterson, B.D.1    Atkins, C.A.2    Graham, D.3    Wills, R.B.H.4
  • 64
    • 0003345999 scopus 로고
    • Histochemistry
    • 3rd. edition Williams and Wilkins Company Baltimore
    • Pearse, A.G.E., Histochemistry. Theoretical and Applied. Volume 1, 3rd. edition, 1968, Williams and Wilkins Company, Baltimore, 759.
    • (1968) Theoretical and Applied , vol.1 , pp. 759
    • Pearse, A.G.E.1
  • 65
    • 84985167969 scopus 로고
    • 3rd. edition Williams and Wilkins Company Baltimore
    • Pearse, A.G.E., 3rd. edition Histochemistry. Theoretical and Applied, 2, 1972, Williams and Wilkins Company, Baltimore, 760–1518.
    • (1972) Histochemistry. Theoretical and Applied , vol.2 , pp. 760-1518
    • Pearse, A.G.E.1
  • 66
    • 0014374602 scopus 로고
    • Ribonuclease isozymes in chinese cabbage, systematically infected with turnip yellow mosaic virus
    • Randles, J.W., Ribonuclease isozymes in chinese cabbage, systematically infected with turnip yellow mosaic virus. Virology 36 (1968), 556–563.
    • (1968) Virology , vol.36 , pp. 556-563
    • Randles, J.W.1
  • 67
  • 68
    • 0039706356 scopus 로고
    • The latency of spinach chloroplast phenolase
    • Sato, M., Hasegawa, M., The latency of spinach chloroplast phenolase. Phytochemistry 15 (1976), 61–65.
    • (1976) Phytochemistry , vol.15 , pp. 61-65
    • Sato, M.1    Hasegawa, M.2
  • 70
    • 0001963447 scopus 로고
    • Genetic control of multiple forms of enzymes in plants: a review
    • Scandalios, J.G., Genetic control of multiple forms of enzymes in plants: a review. Biochem. Genet. 3 (1969), 37–79.
    • (1969) Biochem. Genet. , vol.3 , pp. 37-79
    • Scandalios, J.G.1
  • 71
    • 0018990321 scopus 로고
    • Plant NAD-dependent glutamate dehydrogenase. Purification, molecular properties and metal ion activation of the enzymes from Lemna minor and Pisum sativum
    • Scheid, H.W., Ehmke, A., Hartmann, T., Plant NAD-dependent glutamate dehydrogenase. Purification, molecular properties and metal ion activation of the enzymes from Lemna minor and Pisum sativum. Z. Naturforsch. 35c (1980), 213–221.
    • (1980) Z. Naturforsch. , vol.35 c , pp. 213-221
    • Scheid, H.W.1    Ehmke, A.2    Hartmann, T.3
  • 72
    • 0014265975 scopus 로고
    • Methods for starch-gel electrophoresis of sarcoplasmic proteins
    • Scopes, R.K., Methods for starch-gel electrophoresis of sarcoplasmic proteins. Biochem. J. 107 (1968), 139–150.
    • (1968) Biochem. J. , vol.107 , pp. 139-150
    • Scopes, R.K.1
  • 73
    • 0013830561 scopus 로고
    • The interaction of human serum protein fractions with the starch-iodine complex
    • Searcy, R.L., Hayashi, S., Hardy, E.M., Berk, J.E., The interaction of human serum protein fractions with the starch-iodine complex. Clin. Chim. Acta 12 (1965), 631–638.
    • (1965) Clin. Chim. Acta , vol.12 , pp. 631-638
    • Searcy, R.L.1    Hayashi, S.2    Hardy, E.M.3    Berk, J.E.4
  • 74
    • 0011860256 scopus 로고
    • An appraisal of methods for serum amylase determination
    • Searcy, R.L., Wilding, P., Berk, J.E., An appraisal of methods for serum amylase determination. Clin. Chim. Acta 15 (1967), 189–197.
    • (1967) Clin. Chim. Acta , vol.15 , pp. 189-197
    • Searcy, R.L.1    Wilding, P.2    Berk, J.E.3
  • 75
    • 0000152586 scopus 로고
    • The histochemical demonstration of succinic dehydrogenase
    • Seligman, A.M., Rutenburg, A.M., The histochemical demonstration of succinic dehydrogenase. Science 113 (1951), 317–320.
    • (1951) Science , vol.113 , pp. 317-320
    • Seligman, A.M.1    Rutenburg, A.M.2
  • 76
    • 0014776676 scopus 로고
    • Starch gel electrophoresis of enzymes-A compilation of recipes
    • Shaw, C.R., Prasad, R., Starch gel electrophoresis of enzymes-A compilation of recipes. Biochem. Genet. 4 (1970), 297–320.
    • (1970) Biochem. Genet. , vol.4 , pp. 297-320
    • Shaw, C.R.1    Prasad, R.2
  • 77
    • 0014131442 scopus 로고
    • Ehzym-elektrophorese in einschl- polymerisaten des acrylamids. A. Amylasen, phosphorylasen
    • Siepmann, R., Stegemann, H., Ehzym-elektrophorese in einschl- polymerisaten des acrylamids. A. Amylasen, phosphorylasen. Z. Naturforsch. 22b (1967), 949–955.
    • (1967) Z. Naturforsch. , vol.22 b , pp. 949-955
    • Siepmann, R.1    Stegemann, H.2
  • 78
    • 0010063646 scopus 로고
    • Isozymes of a polyploid series of wheat
    • Sing, C.F., Brewer, G.J., Isozymes of a polyploid series of wheat. Genetics 61 (1969), 391–398.
    • (1969) Genetics , vol.61 , pp. 391-398
    • Sing, C.F.1    Brewer, G.J.2
  • 79
    • 70449155518 scopus 로고
    • Newer knowledge of succinic dehydrogenase
    • Singer, T.P., Kearney, E.B., Massey, V., Newer knowledge of succinic dehydrogenase. Adv. Enzymol. 18 (1957), 65–111.
    • (1957) Adv. Enzymol. , vol.18 , pp. 65-111
    • Singer, T.P.1    Kearney, E.B.2    Massey, V.3
  • 80
    • 0016768222 scopus 로고
    • Reduced nicotinamide adenine dinucleotide-nitrate reductase of Chlorella vulgaris
    • Solomonson, L.P., Lorimer, G.H., Hall, R.L., Borchers, R., Bailey, J.L., Reduced nicotinamide adenine dinucleotide-nitrate reductase of Chlorella vulgaris. J. Biol. Chem 250 (1975), 4120–4127.
    • (1975) J. Biol. Chem , vol.250 , pp. 4120-4127
    • Solomonson, L.P.1    Lorimer, G.H.2    Hall, R.L.3    Borchers, R.4    Bailey, J.L.5
  • 82
    • 0018568045 scopus 로고
    • Linkage, chromosomal association, and expression of Adh-1 and Pgm-2 in tomato
    • Tanksley, S.D., Linkage, chromosomal association, and expression of Adh-1 and Pgm-2 in tomato. Biochem. Genet 17 (1979), 1159–1167.
    • (1979) Biochem. Genet , vol.17 , pp. 1159-1167
    • Tanksley, S.D.1
  • 83
    • 0000489722 scopus 로고
    • Pgi-1 a single gene in tomato responsible for a variable number of isozymes
    • Tanksley, S.D., Pgi-1 a single gene in tomato responsible for a variable number of isozymes. Can. J. Genet. Cytol. 22 (1980), 271–278.
    • (1980) Can. J. Genet. Cytol. , vol.22 , pp. 271-278
    • Tanksley, S.D.1
  • 84
    • 0000169122 scopus 로고
    • Genetics of esterases in species of Lycopersicon
    • Tanksley, S.D., Rick, C.M., Genetics of esterases in species of Lycopersicon. Theor. Appl. Genet. 56 (1980), 209–219.
    • (1980) Theor. Appl. Genet. , vol.56 , pp. 209-219
    • Tanksley, S.D.1    Rick, C.M.2
  • 85
    • 34250260020 scopus 로고
    • Isozymic gene linkage map of the tomato: applications in genetics and breeding
    • Tanksley, S.D., Rick, C.M., Isozymic gene linkage map of the tomato: applications in genetics and breeding. Theor. Appl. Genet 57 (1980), 161–170.
    • (1980) Theor. Appl. Genet , vol.57 , pp. 161-170
    • Tanksley, S.D.1    Rick, C.M.2
  • 86
    • 0348206861 scopus 로고
    • A method for the localization of catalase on starch gels
    • Thorup, O.A., Strole, W.B., Leavell, B.S., A method for the localization of catalase on starch gels. J. Lab. Clin. Med. 58 (1961), 122–128.
    • (1961) J. Lab. Clin. Med. , vol.58 , pp. 122-128
    • Thorup, O.A.1    Strole, W.B.2    Leavell, B.S.3
  • 87
    • 0014415484 scopus 로고
    • Peroxidase activity of hemepeptides from horse heart cytochrome c
    • Tu, A.T., Reinosa, J.A., Hsiao, Y.Y., Peroxidase activity of hemepeptides from horse heart cytochrome c. Experientia 24 (1968), 219–221.
    • (1968) Experientia , vol.24 , pp. 219-221
    • Tu, A.T.1    Reinosa, J.A.2    Hsiao, Y.Y.3
  • 88
    • 77956980970 scopus 로고
    • Starch gel electrophoresis of plant NADH-nitrate reductase and nitrite reductase
    • Upcroft, J.A., Done, J., Starch gel electrophoresis of plant NADH-nitrate reductase and nitrite reductase. J. Exp. Bot. 25 (1974), 503–508.
    • (1974) J. Exp. Bot. , vol.25 , pp. 503-508
    • Upcroft, J.A.1    Done, J.2
  • 89
    • 49949121479 scopus 로고
    • The identification of myrosinase after the elctrophoresis of Brassica and Sinapis
    • Vaughan, J.G., Gordon, E., Robinson, D., The identification of myrosinase after the elctrophoresis of Brassica and Sinapis. Seed proteins. Phytochemistry 7 (1968), 1345–1348.
    • (1968) Seed proteins. Phytochemistry , vol.7 , pp. 1345-1348
    • Vaughan, J.G.1    Gordon, E.2    Robinson, D.3
  • 90
    • 0001871213 scopus 로고
    • Glycosidases in cell wall-degrading extracts of ripening tomato fruits
    • Wallner, S.J., Walker, J.E., Glycosidases in cell wall-degrading extracts of ripening tomato fruits. Plant Physiol. 55 (1975), 94–98.
    • (1975) Plant Physiol. , vol.55 , pp. 94-98
    • Wallner, S.J.1    Walker, J.E.2


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