메뉴 건너뛰기




Volumn , Issue , 2002, Pages 1-555

Handbook of detection of enzymes on electrophoretic gels, second edition

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85057488290     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Book
Times cited : (48)

References (116)
  • 1
    • 0000152586 scopus 로고
    • The histochemical demonstration of succinic dehydrogenase
    • Seligman, A.M. and Rutenberg, A.M., The histochemical demonstration of succinic dehydrogenase, Science, 113, 317, 1951.
    • (1951) Science , vol.113 , pp. 317
    • Seligman, A.M.1    Rutenberg, A.M.2
  • 2
    • 0000535586 scopus 로고
    • Multiple forms of enzymes: Tissue, ontogenetic, and species speciÞc patterns
    • Markert, C.L. and Möller, F., Multiple forms of enzymes: tissue, ontogenetic, and species speciÞc patterns, Proc. Natl. Acad. Sci. U.S.A., 45, 753, 1959.
    • (1959) Proc. Natl. Acad. Sci. U.S.A. , vol.45 , pp. 753
    • Markert, C.L.1    Möller, F.2
  • 5
    • 0001362081 scopus 로고
    • Histochemical demonstration of enzymes separated by zone electrophoresis in starch gels
    • Hunter, R.L. and Markert, C.L., Histochemical demonstration of enzymes separated by zone electrophoresis in starch gels, Science, 125, 1294, 1957.
    • (1957) Science , vol.125 , pp. 1294
    • Hunter, R.L.1    Markert, C.L.2
  • 8
    • 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, 23, 1939.
    • (1939) Proc. Soc. Exp. Biol. Med. , vol.42 , pp. 23
    • Gomori, G.1
  • 9
    • 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, 189, 1941.
    • (1941) Arch. Pathol. , vol.32 , pp. 189
    • Gomori, G.1
  • 10
    • 0020482814 scopus 로고
    • 2 after polyacrylamide gel electrophoresis
    • 2 after polyacrylamide gel electrophoresis, Anal. Biochem., 121, 17, 1982.
    • (1982) Anal. Biochem. , vol.121 , pp. 17
    • Nimmo, H.G.1    Nimmo, G.A.2
  • 11
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske, C.H. and Subbarow, Y., The colorimetric determination of phosphorus, J. Biol. Chem., 66, 375, 1925.
    • (1925) J. Biol. Chem. , vol.66 , pp. 375
    • Fiske, C.H.1    Subbarow, Y.2
  • 13
    • 0022578931 scopus 로고
    • A sensitive staining technique for the detection of phosphohydrolase activities after polyacrylamide gel electrophoresis
    • Zlotnick, G.W. and Gottlieb, M., A sensitive staining technique for the detection of phosphohydrolase activities after polyacrylamide gel electrophoresis, Anal. Biochem., 153, 121, 1986.
    • (1986) Anal. Biochem. , vol.153 , pp. 121
    • Zlotnick, G.W.1    Gottlieb, M.2
  • 14
    • 0019850575 scopus 로고
    • Visualization of isozymes which generate inorganic phosphate
    • Klebe, R.J., Schloss, S., Mock, L., and Link, C.R., Visualization of isozymes which generate inorganic phosphate, Biochem. Genet., 19, 921, 1981.
    • (1981) Biochem. Genet. , vol.19 , pp. 921
    • Klebe, R.J.1    Schloss, S.2    Mock, L.3    Link, C.R.4
  • 15
    • 0018385979 scopus 로고
    • ModiÞ-cations in the enzymatic assay for inorganic phosphate
    • Cornell, N.W., Leadbetter, M.G., and Veech, R.L., ModiÞ-cations in the enzymatic assay for inorganic phosphate, Anal. Biochem., 95, 524, 1979.
    • (1979) Anal. Biochem. , vol.95 , pp. 524
    • Cornell, N.W.1    Leadbetter, M.G.2    Veech, R.L.3
  • 16
    • 0001011257 scopus 로고
    • Effects of adenylic acid on the kinetics of muscle phosphorylase a
    • 1964
    • Lowry, O.H., Schulz, D.W., and Passoneau, J.V., Effects of adenylic acid on the kinetics of muscle phosphorylase a, J. Biol. Chem., 239, 1947, 1964.
    • (1947) J. Biol. Chem. , vol.239
    • Lowry, O.H.1    Schulz, D.W.2    Passoneau, J.V.3
  • 17
    • 0348206861 scopus 로고
    • A method for the localization of catalase on starch gels
    • Thorup, O.A., Strole, W.B., and Leavell, B.S., A method for the localization of catalase on starch gels, J. Lab. Clin. Med., 58, 122, 1961.
    • (1961) J. Lab. Clin. Med. , vol.58 , pp. 122
    • Thorup, O.A.1    Strole, W.B.2    Leavell, B.S.3
  • 18
    • 0022648398 scopus 로고
    • Enzy-moblotting: A method for localizing proteinases and their zymogens using para-nitroanilide substrates after agarose gel electrophoresis and transfer to nitrocellulose
    • Ohlsson, B.G., Weström, B.R., and Karlsson, B.W., Enzy-moblotting: a method for localizing proteinases and their zymogens using para-nitroanilide substrates after agarose gel electrophoresis and transfer to nitrocellulose, Anal. Biochem., 152, 239, 1986.
    • (1986) Anal. Biochem. , vol.152 , pp. 239
    • Ohlsson, B.G.1    Weström, B.R.2    Karlsson, B.W.3
  • 19
    • 0020839760 scopus 로고
    • Polyacrylamide gels which contain a novel mixed disulÞde compound can be used to detect enzymes that catalyze thiol-producing reactions
    • Harris, R.B. and Wilson, I.B., Polyacrylamide gels which contain a novel mixed disulÞde compound can be used to detect enzymes that catalyze thiol-producing reactions, Anal. Biochem., 134, 126, 1983.
    • (1983) Anal. Biochem. , vol.134 , pp. 126
    • Harris, R.B.1    Wilson, I.B.2
  • 20
    • 0019976518 scopus 로고
    • A direct method for the visualization of glu-tathione S-transferase activity in polyacrylamide gels
    • Clark, A.G., A direct method for the visualization of glu-tathione S-transferase activity in polyacrylamide gels, Anal. Biochem., 123, 147, 1982.
    • (1982) Anal. Biochem. , vol.123 , pp. 147
    • Clark, A.G.1
  • 21
    • 0000372407 scopus 로고
    • Time-resolved ßuorescence detection of enzyme-ampliÞed lanthanide luminescence for nucleic acid hybridization assays
    • Templeton, E.F.G., Wong, H.E., Evangelista, R.A., Granger, T., and Pollak, A., Time-resolved ßuorescence detection of enzyme-ampliÞed lanthanide luminescence for nucleic acid hybridization assays, Clin. Chem., 37, 1506, 1991.
    • (1991) Clin. Chem. , vol.37 , pp. 1506
    • Templeton, E.F.G.1    Wong, H.E.2    Evangelista, R.A.3    Granger, T.4    Pollak, A.5
  • 22
    • 0025783280 scopus 로고
    • Enzyme-ampliÞed lanthanide luminescence for enzyme detection in bioanalytical assays
    • Evangelista, R.A., Pollak, A., and Templeton, E.F.G., Enzyme-ampliÞed lanthanide luminescence for enzyme detection in bioanalytical assays, Anal. Biochem., 197, 213, 1991.
    • (1991) Anal. Biochem. , vol.197 , pp. 213
    • Evangelista, R.A.1    Pollak, A.2    Templeton, E.F.G.3
  • 24
    • 0017707728 scopus 로고
    • Bioautography: A general method for the visualization of enzymes
    • Naylor, S.L. and Klebe, R.J., Bioautography: a general method for the visualization of enzymes, Biochem. Genet., 15, 1193, 1977.
    • (1977) Biochem. Genet. , vol.15 , pp. 1193
    • Naylor, S.L.1    Klebe, R.J.2
  • 25
    • 0019099291 scopus 로고
    • Bioautographic visualization of enzymes
    • Vol., Rattazzi, M.C., Scandalios, J.G., and Whitt, G.S., Eds., Alan R. Liss, New York, p
    • Naylor, S.L., Bioautographic visualization of enzymes, in Isozymes: Current Topics in Biological and Medical Research, Vol. 4, Rattazzi, M.C., Scandalios, J.G., and Whitt, G.S., Eds., Alan R. Liss, New York, 1980, p. 69.
    • (1980) Isozymes: Current Topics in Biological and Medical Research , vol.4 , pp. 69
    • Naylor, S.L.1
  • 26
  • 29
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications, Proc. Natl. Acad. Sci. U.S.A., 76, 4350, 1979.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 30
    • 0019551730 scopus 로고
    • “Western blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate–polyacrylamide gels to unmodiÞed nitrocellulose and radiographic detection with antibody and radiolabeled protein A
    • Burnette, W.N., “Western blotting”: electrophoretic transfer of proteins from sodium dodecyl sulfate–polyacrylamide gels to unmodiÞed nitrocellulose and radiographic detection with antibody and radiolabeled protein A, Anal. Biochem., 112, 195, 1981.
    • (1981) Anal. Biochem. , vol.112 , pp. 195
    • Burnette, W.N.1
  • 31
    • 0020579390 scopus 로고
    • Protein blotting: Principles and applications
    • Gershoni, J.M. and Palade, G.E., Protein blotting: principles and applications, Anal. Biochem., 131, 1, 1983.
    • (1983) Anal. Biochem. , vol.131 , Issue.1
    • Gershoni, J.M.1    Palade, G.E.2
  • 33
    • 0016700864 scopus 로고
    • Detection of speciÞc sequences among DNA fragments separated by gel electrophoresis
    • Southern, E.M., Detection of speciÞc sequences among DNA fragments separated by gel electrophoresis, J. Mol. Biol., 98, 503, 1975.
    • (1975) J. Mol. Biol. , vol.98 , pp. 503
    • Southern, E.M.1
  • 34
    • 0035476480 scopus 로고    scopus 로고
    • Direct immunode-tection of antigens within the precast polyacrylamide gel
    • Desai, S., Dworecki, B., and Cichon, E., Direct immunode-tection of antigens within the precast polyacrylamide gel, Anal. Biochem., 297, 94, 2001.
    • (2001) Anal. Biochem. , vol.297 , pp. 94
    • Desai, S.1    Dworecki, B.2    Cichon, E.3
  • 35
    • 0022016104 scopus 로고
    • Monoclonal antibodies in enzyme research: Present and potential applications
    • Vora, S., Monoclonal antibodies in enzyme research: present and potential applications, Anal. Biochem., 144, 307, 1985.
    • (1985) Anal. Biochem. , vol.144 , pp. 307
    • Vora, S.1
  • 36
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predeÞned speciÞcity
    • Köhler, G. and Milstein, C., Continuous cultures of fused cells secreting antibody of predeÞned speciÞcity, Nature, 256, 495, 1975.
    • (1975) Nature , vol.256 , pp. 495
    • Köhler, G.1    Milstein, C.2
  • 39
    • 0023428651 scopus 로고
    • A method for the production of highly speciÞc polyclonal antibodies
    • Diano, M., Le Bivic, A., and Hirn, M., A method for the production of highly speciÞc polyclonal antibodies, Anal. Biochem., 166, 224, 1987.
    • (1987) Anal. Biochem. , vol.166 , pp. 224
    • Diano, M.1    Le Bivic, A.2    Hirn, M.3
  • 40
    • 0021321955 scopus 로고
    • A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots
    • Blake, M.S., Johnston, K.H., Russell-Jones, G.J., and Gotschlich, E.C., A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots, Anal. Biochem., 136, 175, 1984.
    • (1984) Anal. Biochem. , vol.136 , pp. 175
    • Blake, M.S.1    Johnston, K.H.2    Russell-Jones, G.J.3    Gotschlich, E.C.4
  • 41
    • 0022202132 scopus 로고
    • Phenols as enhancers of the chemiluminescent horseradish peroxidase–luminol–hydrogen peroxide reaction: Application in luminescence-monitored enzyme immunoas-says
    • Thorpe, G.H.G., Kricka, L.J., Moseley, S.B., and Whitehead, T.P., Phenols as enhancers of the chemiluminescent horseradish peroxidase–luminol–hydrogen peroxide reaction: application in luminescence-monitored enzyme immunoas-says, Clin. Chem., 31, 1335, 1985.
    • (1985) Clin. Chem. , vol.31 , pp. 1335
    • Thorpe, G.H.G.1    Kricka, L.J.2    Moseley, S.B.3    Whitehead, T.P.4
  • 42
    • 0004044082 scopus 로고
    • Bjerrun, O.G. and Heegaard, N.H.H., Eds., CRC Press, Boca Raton, FL
    • Bjerrun, O.G. and Heegaard, N.H.H., Eds., CRC Handbook of Immunoblotting of Proteins, CRC Press, Boca Raton, FL, 1988.
    • (1988) CRC Handbook of Immunoblotting of Proteins
  • 43
    • 84902237445 scopus 로고    scopus 로고
    • Pound, J., Ed., Humana Press, Totowa, NJ
    • Pound, J., Ed., Immunochemical Protocols, Humana Press, Totowa, NJ, 1998.
    • (1998) Immunochemical Protocols
  • 44
    • 0028921828 scopus 로고
    • Activity staining of xylanases in polyacrylamide gels containing xylan
    • Chen, P. and Buller, C.S., Activity staining of xylanases in polyacrylamide gels containing xylan, Anal. Biochem., 226, 186, 1995.
    • (1995) Anal. Biochem. , vol.226 , pp. 186
    • Chen, P.1    Buller, C.S.2
  • 45
    • 0031554897 scopus 로고    scopus 로고
    • TLC blotting: Application to microscale analysis of lipids and as a new approach to lipid–protein interaction
    • Taki, T. and Ishikawa, D., TLC blotting: application to microscale analysis of lipids and as a new approach to lipid–protein interaction, Anal. Biochem., 251, 135, 1997.
    • (1997) Anal. Biochem. , vol.251 , pp. 135
    • Taki, T.1    Ishikawa, D.2
  • 46
    • 0025810945 scopus 로고
    • Characterization of DNA metabolizing enzymes in situ following polyacrylamide gel electrophoresis
    • Longley, M.J. and Mosbaugh, D.W., Characterization of DNA metabolizing enzymes in situ following polyacrylamide gel electrophoresis, Biochemistry, 30, 2655, 1991.
    • (1991) Biochemistry , vol.30 , pp. 2655
    • Longley, M.J.1    Mosbaugh, D.W.2
  • 47
    • 0027326063 scopus 로고
    • W., In situ detection of DNA-metabolizing enzymes following polyacrylamide gel electrophoresis
    • Longley, M.J. and Mosbaugh, D.W., In situ detection of DNA-metabolizing enzymes following polyacrylamide gel electrophoresis, Methods Enzymol., 218, 587, 1993.
    • (1993) Methods Enzymol , vol.218 , pp. 587
    • Longley, M.J.1    Mosbaugh, D.2
  • 48
    • 0027316867 scopus 로고
    • Activity gel and activity blotting methods for detecting DNA-modifying (Repair) enzymes
    • Seki, S., Akiyama, K., Watanabe, S., and Tsutsui, K., Activity gel and activity blotting methods for detecting DNA-modifying (repair) enzymes, J. Chromatogr., 618, 147, 1993.
    • (1993) J. Chromatogr. , vol.618 , Issue.147
    • Seki, S.1    Akiyama, K.2    Watanabe, S.3    Tsutsui, K.4
  • 49
    • 0029437393 scopus 로고
    • Conformational properties of oligonucleotides
    • Gold, L., Conformational properties of oligonucleotides, Nucleic Acids Symp. Ser., 33, 20, 1995.
    • (1995) Nucleic Acids Symp. Ser. , vol.33 , pp. 20
    • Gold, L.1
  • 50
    • 0031152065 scopus 로고    scopus 로고
    • Aptamers as therapeutic and diagnostic reagents: Problems and prospects
    • Osborne, S.E., Matsumura, I., and Ellington, A.D., Aptamers as therapeutic and diagnostic reagents: problems and prospects, Curr. Opin. Chem. Biol., 1, 5, 1997.
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 5
    • Osborne, S.E.1    Matsumura, I.2    Ellington, A.D.3
  • 51
    • 0033027625 scopus 로고    scopus 로고
    • Aptamers as tools in molecular biology and immunology
    • Famulok, M. and Mayer, G., Aptamers as tools in molecular biology and immunology, Curr. Top. Microbiol. Immunol., 243, 123, 1999.
    • (1999) Curr. Top. Microbiol. Immunol. , vol.243 , pp. 123
    • Famulok, M.1    Mayer, G.2
  • 52
    • 0026575221 scopus 로고
    • Selection of single-stranded DNA molecules that bind and inhibit human thrombin
    • Bock, L.C., GrifÞn, L.C., Latham, J.A., Vermaas, E.H., and Toole, J.J., Selection of single-stranded DNA molecules that bind and inhibit human thrombin, Nature, 355, 564, 1992.
    • (1992) Nature , vol.355 , pp. 564
    • Bock, L.C.1    Grifþn, L.C.2    Latham, J.A.3    Vermaas, E.H.4    Toole, J.J.5
  • 53
    • 0030589094 scopus 로고    scopus 로고
    • Detecting immobilized protein kinase C isozymes with RNA aptamers
    • Conrad, R. and Ellington, A.D., Detecting immobilized protein kinase C isozymes with RNA aptamers, Anal. Biochem., 242, 261, 1996.
    • (1996) Anal. Biochem. , vol.242 , pp. 261
    • Conrad, R.1    Ellington, A.D.2
  • 54
    • 0035879386 scopus 로고    scopus 로고
    • Aptamer beacons for the direct detection of proteins
    • Hamaguchi, N., Ellington, A., and Stanton, M., Aptamer beacons for the direct detection of proteins, Anal. Biochem., 294, 126, 2001.
    • (2001) Anal. Biochem. , vol.294 , pp. 126
    • Hamaguchi, N.1    Ellington, A.2    Stanton, M.3
  • 55
    • 0029161894 scopus 로고
    • Biotinylated aprotinin: A versatile probe for the detection of serine proteinases on Western blots
    • Melrose, J., Ghosh, P., and Patel, M., Biotinylated aprotinin: a versatile probe for the detection of serine proteinases on Western blots, Int. J. Biochem. Cell Biol., 27, 891, 1995.
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 891
    • Melrose, J.1    Ghosh, P.2    Patel, M.3
  • 56
    • 0028997493 scopus 로고
    • Biotin-labeled potato chymotrypsin inhibitor-1: A useful probe for the detection and quantitation of chymotrypsin-like serine proteinases on Western blots and its application in the detection of a serine proteinase synthesized by articular chondrocytes
    • Rodgers, K.J., Melrose, J., and Ghosh, P., Biotin-labeled potato chymotrypsin inhibitor-1: a useful probe for the detection and quantitation of chymotrypsin-like serine proteinases on Western blots and its application in the detection of a serine proteinase synthesized by articular chondrocytes, Anal. Biochem., 227, 129, 1995.
    • (1995) Anal. Biochem. , vol.227 , pp. 129
    • Rodgers, K.J.1    Melrose, J.2    Ghosh, P.3
  • 57
    • 0031024924 scopus 로고    scopus 로고
    • Quantitative reverse zymography: Analysis of picogram amounts of metalloproteinase inhibitors using gelatinase A and B reverse zymograms
    • Oliver, G.W., Leferson, J.D., Stetler-Stevenson, W.G., and Kleiner, D.E., Quantitative reverse zymography: analysis of picogram amounts of metalloproteinase inhibitors using gelatinase A and B reverse zymograms, Anal. Biochem., 244, 161, 1997.
    • (1997) Anal. Biochem. , vol.244 , pp. 161
    • Oliver, G.W.1    Leferson, J.D.2    Stetler-Stevenson, W.G.3    Kleiner, D.E.4
  • 58
    • 0029066738 scopus 로고
    • Activity staining of mammalian ribonuclease inhibitors after electrophoresis in sealed vertical slab polyacrylamide gels
    • Nadano, D., Yasuda, T., Takeshita, H., and Kishi, K., Activity staining of mammalian ribonuclease inhibitors after electrophoresis in sealed vertical slab polyacrylamide gels, Anal. Biochem., 227, 210, 1995.
    • (1995) Anal. Biochem. , vol.227 , pp. 210
    • Nadano, D.1    Yasuda, T.2    Takeshita, H.3    Kishi, K.4
  • 59
    • 0028080140 scopus 로고
    • The preparation and use of biotinylated trypsin in Western blotting for detection of trypsin inhibitory proteins
    • Melrose, J., Rodgers, K., and Ghosh, P., The preparation and use of biotinylated trypsin in Western blotting for detection of trypsin inhibitory proteins, Anal. Biochem., 222, 34, 1994.
    • (1994) Anal. Biochem. , vol.222 , pp. 34
    • Melrose, J.1    Rodgers, K.2    Ghosh, P.3
  • 60
    • 0030021415 scopus 로고    scopus 로고
    • Biotinylated trypsin and its application as a sensitive, versatile probe for the detection and characterisation of an ovine chondrocyte serine proteinase inhibitor using Western blotting
    • Rodgers, K.J., Melrose, J., and Ghosh, P., Biotinylated trypsin and its application as a sensitive, versatile probe for the detection and characterisation of an ovine chondrocyte serine proteinase inhibitor using Western blotting, Electrophoresis, 17, 213, 1996.
    • (1996) Electrophoresis , vol.17 , pp. 213
    • Rodgers, K.J.1    Melrose, J.2    Ghosh, P.3
  • 61
    • 0030046593 scopus 로고    scopus 로고
    • Biotinylated hyaluronan: A versatile and highly sensitive probe capable of detecting nanogram levels of hyaluronan binding proteins (hyaloadherins) on electroblots by a novel afÞnity detection procedure
    • Melrose, J., Numata, Y., and Ghosh, P., Biotinylated hyaluronan: a versatile and highly sensitive probe capable of detecting nanogram levels of hyaluronan binding proteins (hyaloadherins) on electroblots by a novel afÞnity detection procedure, Electrophoresis, 17, 205, 1996.
    • (1996) Electrophoresis , vol.17 , pp. 205
    • Melrose, J.1    Numata, Y.2    Ghosh, P.3
  • 63
    • 37049163529 scopus 로고
    • A new apparatus for electrophoretic analysis of colloidal mixtures
    • Tiselius, A., A new apparatus for electrophoretic analysis of colloidal mixtures, Trans. Faraday Soc., 33, 524, 1937.
    • (1937) Trans. Faraday Soc. , vol.33 , pp. 524
    • Tiselius, A.1
  • 64
    • 0345582990 scopus 로고
    • Zone electrophoresis in starch gels: Group variations in the serum proteins of normal human adults
    • Smithies, O., Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults, Biochem. J., 61, 629, 1955.
    • (1955) Biochem. J. , vol.61 , pp. 629
    • Smithies, O.1
  • 65
    • 0000609886 scopus 로고
    • A cellulose acetate supporting medium for zone electrophoresis
    • Kohn, J., A cellulose acetate supporting medium for zone electrophoresis, Clin. Chim. Acta, 2, 297, 1957.
    • (1957) Clin. Chim. Acta , vol.2 , pp. 297
    • Kohn, J.1
  • 67
    • 0001602958 scopus 로고
    • Acrylamide gel as a supporting medium for zone electrophoresis
    • Raymond, S. and Weintraub, L., Acrylamide gel as a supporting medium for zone electrophoresis, Science, 130, 711, 1959.
    • (1959) Science , vol.130 , pp. 711
    • Raymond, S.1    Weintraub, L.2
  • 69
    • 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, 23, 1939.
    • (1939) Proc. Soc. Exp. Biol. Med. , vol.42 , pp. 23
    • Gomori, G.1
  • 73
    • 0001362081 scopus 로고
    • Histochemical demonstration of enzymes separated by zone electrophoresis in starch gels
    • Hunter, R.L. and Markert, C.L., Histochemical demonstration of enzymes separated by zone electrophoresis in starch gels, Science, 125, 1294, 1957.
    • (1957) Science , vol.125 , pp. 1294
    • Hunter, R.L.1    Markert, C.L.2
  • 74
    • 0000535586 scopus 로고
    • Multiple forms of enzymes: Tissue, ontogenetic, and species speciÞc patterns
    • Markert, C.L. and Möller, F., Multiple forms of enzymes: tissue, ontogenetic, and species speciÞc patterns, Proc. Natl. Acad. Sci. U.S.A., 45, 753, 1959.
    • (1959) Proc. Natl. Acad. Sci. U.S.A. , vol.45 , pp. 753
    • Markert, C.L.1    Möller, F.2
  • 78
    • 0019208428 scopus 로고
    • A survey on the formation and localization of secondary isozymes in mammalian
    • Rothe, G.M., A survey on the formation and localization of secondary isozymes in mammalian, Hum. Genet., 56, 129, 1980.
    • (1980) Hum. Genet. , vol.56 , pp. 129
    • Rothe, G.M.1
  • 79
    • 0003786397 scopus 로고
    • Chapman & Hall Ltd., London
    • Moss, D.W., Isoenzymes, Chapman & Hall Ltd., London, 1982.
    • (1982) Isoenzymes
    • Moss, D.W.1
  • 81
    • 0002146711 scopus 로고
    • Genetic principles and the interpretation of electrophoretic data
    • Whitmore, D.H., Ed., CRC Press, Boca Raton, FL, p
    • Buth, D.G., Genetic principles and the interpretation of electrophoretic data, in Electrophoretic and Isoelectric Focusing Techniques in Fisheries Management, Whitmore, D.H., Ed., CRC Press, Boca Raton, FL, 1990, p. 1.
    • (1990) Electrophoretic and Isoelectric Focusing Techniques in Fisheries Management , pp. 1
    • Buth, D.G.1
  • 82
    • 84910553152 scopus 로고
    • Nomenclature of multiple forms of enzymes: Recommendations (1976)
    • IUPAC-IUB Commission on Biochemical Nomenclature, Nomenclature of multiple forms of enzymes: recommendations (1976), J. Biol. Chem., 252, 5939, 1977.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5939
  • 84
    • 0003450992 scopus 로고
    • Academic Press, San Diego
    • NC-IUBMB, Enzyme Nomenclature, Academic Press, San Diego, 1992.
    • (1992) Enzyme Nomenclature
  • 85
    • 0017707728 scopus 로고
    • Bioautography: A general method for the visualization of enzymes
    • Naylor, S.L. and Klebe, R.L., Bioautography: a general method for the visualization of enzymes, Biochem. Genet., 15, 1193, 1977.
    • (1977) Biochem. Genet. , vol.15 , pp. 1193
    • Naylor, S.L.1    Klebe, R.L.2
  • 86
  • 87
    • 0022016104 scopus 로고
    • Monoclonal antibodies in enzyme research: Present and potential applications
    • Vora, S., Monoclonal antibodies in enzyme research: present and potential applications, Anal. Biochem., 144, 307, 1985.
    • (1985) Anal. Biochem. , vol.144 , pp. 307
    • Vora, S.1
  • 91
    • 0001872764 scopus 로고    scopus 로고
    • Molecular Systematics, Hillis, D.M., Moritz, C., and Mable, B.K., Eds., Sinauer, Sunderland, p
    • Murphy, R.W., Sites, J.W., Jr., Buth, D.G., and Haußer, C.H., Proteins: isozyme electrophoresis, in Molecular Systematics, Hillis, D.M., Moritz, C., and Mable, B.K., Eds., Sinauer, Sunderland, 1996, p. 51.
    • (1996) Proteins: Isozyme Electrophoresis , pp. 51
    • Murphy, R.W.1    Sites, J.W.2    Buth, D.G.3    Haußer, C.H.4
  • 92
    • 0003159168 scopus 로고    scopus 로고
    • Starch gel electrophoresis of allozymes
    • 2nd ed., Hoelzel, A.R., Ed., Oxford University Press, Oxford, p
    • May, B., Starch gel electrophoresis of allozymes, in Molecular Genetic Analysis of Populations: A Practical Approach, 2nd ed., Hoelzel, A.R., Ed., Oxford University Press, Oxford, 1998, p. 1.
    • (1998) Molecular Genetic Analysis of Populations: A Practical Approach , pp. 1
    • May, B.1
  • 93
    • 85057479275 scopus 로고
    • Practical Protein Electrophoresis for Genetic Research
    • Acquaah, G., Practical Protein Electrophoresis for Genetic Research, Timber Press, Portland, OR, 1992.
    • (1992) Timber Press, Portland, OR
    • Acquaah, G.1
  • 95
    • 0000135366 scopus 로고
    • Subunit structure of enzymes: Allozymic data
    • Manchenko, G.P., Subunit structure of enzymes: allozymic data, Isozyme Bull., 21, 144, 1988.
    • (1988) Isozyme Bull , vol.21 , pp. 144
    • Manchenko, G.P.1
  • 96
    • 85057490348 scopus 로고    scopus 로고
    • Humana Press, Totowa, NJ
    • Lieber, D.C., Proteomics, Humana Press, Totowa, NJ, 2001.
    • (2001) Proteomics
    • Lieber, D.C.1
  • 99
    • 0035895505 scopus 로고    scopus 로고
    • 274 coauthors, The sequence of the human genome
    • Venter, J.C., Adams, M.D., Myers, E.W., and 274 coauthors, The sequence of the human genome, Science, 291, 1304, 2001.
    • (2001) Science , vol.291 , pp. 1304
    • Venter, J.C.1    Adams, M.D.2    Myers, E.W.3
  • 100
    • 0031900540 scopus 로고    scopus 로고
    • The evolution of the alcohol dehydrogenase gene family by loss of introns in plants of the genus Leavenworthia (Brassicaceae)
    • Charlesworth, D., Liu, F.-L., and Zhang L., The evolution of the alcohol dehydrogenase gene family by loss of introns in plants of the genus Leavenworthia (Brassicaceae), Mol. Biol. Evol., 15, 552, 1998.
    • (1998) Mol. Biol. Evol. , vol.15 , pp. 552
    • Charlesworth, D.1    Liu, F.-L.2    Zhang, L.3
  • 102
    • 0033784598 scopus 로고    scopus 로고
    • Isozyme pattern of glycogen phosphorylase in the rat nervous system and rat astroglia-rich primary cultures: Electrophoretic and polymerase chain reaction studies
    • Pfeiffer-Guglielmi, B., Broer, S., Broer, A., and Hamprecht, B., Isozyme pattern of glycogen phosphorylase in the rat nervous system and rat astroglia-rich primary cultures: electrophoretic and polymerase chain reaction studies, Neurochem. Res., 25, 1485, 2000.
    • (2000) Neurochem. Res. , vol.25 , pp. 1485
    • Pfeiffer-Guglielmi, B.1    Broer, S.2    Broer, A.3    Hamprecht, B.4
  • 103
    • 0031804062 scopus 로고    scopus 로고
    • A new method for the detection of hydantoinases with respect to their enanti-oselectivity on acrylamide gels based on enzyme activity stain
    • May, O., Siemann, M., and Syldatk, C., A new method for the detection of hydantoinases with respect to their enanti-oselectivity on acrylamide gels based on enzyme activity stain, Biotechnol. Tech., 12, 309, 1998.
    • (1998) Biotechnol. Tech. , vol.12 , pp. 309
    • May, O.1    Siemann, M.2    Syldatk, C.3
  • 104
    • 0035099328 scopus 로고    scopus 로고
    • Cloning and characterization of the gene encoding the glutamate dehydrogenase of Streptococcus suis serotype 2
    • Okwumabua, O., Persaud, J.S., and Reddy, P.G., Cloning and characterization of the gene encoding the glutamate dehydrogenase of Streptococcus suis serotype 2, Clin. Diagn. Lab. Immun., 8, 251, 2001.
    • (2001) Clin. Diagn. Lab. Immun. , vol.8 , pp. 251
    • Okwumabua, O.1    Persaud, J.S.2    Reddy, P.G.3
  • 105
    • 0034759693 scopus 로고    scopus 로고
    • Stromelysin gene transfer into cultured human trabecular cells and rat trabecular meshwork in vivo
    • Kee, C., Sohn, S., and Hwang, J.M., Stromelysin gene transfer into cultured human trabecular cells and rat trabecular meshwork in vivo, Invest. Ophthalmol. Vis. Sci., 42, 2856, 2001.
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , pp. 2856
    • Kee, C.1    Sohn, S.2    Hwang, J.M.3
  • 107
    • 0028142375 scopus 로고
    • From electrophoretically separated protein to identiÞcation: Strategies for sequence and mass analysis
    • Patterson, S.D., From electrophoretically separated protein to identiÞcation: strategies for sequence and mass analysis, Anal. Biochem., 221, 1, 1994.
    • (1994) Anal. Biochem. , vol.221 , Issue.1
    • Patterson, S.D.1
  • 108
    • 0034721644 scopus 로고    scopus 로고
    • Protein diversity from alternative splicing: A challenge for bioinformatics and post-genome biology
    • Black, D.L., Protein diversity from alternative splicing: a challenge for bioinformatics and post-genome biology, Cell, 103, 367, 2000.
    • (2000) Cell , vol.103 , pp. 367
    • Black, D.L.1
  • 109
  • 110
    • 0141861525 scopus 로고    scopus 로고
    • Isozymes generated via alternative splicing of pre-mRNAs transcribed from single genes
    • Manchenko, G.P., Isozymes generated via alternative splicing of pre-mRNAs transcribed from single genes, Gene Fam. Isozymes Bull., 34, 12, 2001.
    • (2001) Gene Fam. Isozymes Bull. , vol.34 , pp. 12
    • Manchenko, G.P.1
  • 111
    • 0034794927 scopus 로고    scopus 로고
    • Unusual isozyme patterns of glucose-6-phosphate isomerase in Polydora brevipalpa (Polychaeta: Spionidae)
    • Manchenko, G.P., Unusual isozyme patterns of glucose-6-phosphate isomerase in Polydora brevipalpa (Polychaeta: Spionidae), Biochem. Genet., 39, 285, 2001.
    • (2001) Biochem. Genet. , vol.39 , pp. 285
    • Manchenko, G.P.1
  • 112
    • 0021770685 scopus 로고
    • Heterogeneity of mammalian DNA ligase detected on activity and DNA sequencing gels
    • Mezzina, M., Sarasin, A., Politi, N., and Bertazzoni, U., Heterogeneity of mammalian DNA ligase detected on activity and DNA sequencing gels, Nucleic Acids Res., 12, 5109, 1984.
    • (1984) Nucleic Acids Res , vol.12 , Issue.5109
    • Mezzina, M.1    Sarasin, A.2    Politi, N.3    Bertazzoni, U.4
  • 113
    • 0025810945 scopus 로고
    • Characterization of DNA metabolizing enzymes in situ following polyacrylamide gel electrophoresis
    • Longley, M.J. and Mosbaugh, D.W., Characterization of DNA metabolizing enzymes in situ following polyacrylamide gel electrophoresis, Biochemistry, 30, 2655, 1991.
    • (1991) Biochemistry , vol.30 , pp. 2655
    • Longley, M.J.1    Mosbaugh, D.W.2
  • 114
    • 0027326063 scopus 로고
    • W., In situ detection of DNA-metabolizing enzymes following polyacrylamide gel electrophoresis
    • Longley, M.J. and Mosbaugh, D.W., In situ detection of DNA-metabolizing enzymes following polyacrylamide gel electrophoresis, Methods Enzymol., 218, 587, 1993.
    • (1993) Methods Enzymol , vol.218 , pp. 587
    • Longley, M.J.1    Mosbaugh, D.2
  • 115
    • 0023613953 scopus 로고
    • Rapid and efÞcient site-speciÞc mutagenesis without phenotypic selection
    • Kunkel, T.A., Roberts, J.D., and Zakour, R.A., Rapid and efÞcient site-speciÞc mutagenesis without phenotypic selection, Methods Enzymol., 154, 367, 1987.
    • (1987) Methods Enzymol , vol.154 , pp. 367
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 116
    • 85057481578 scopus 로고
    • San Diego, EC 6.5.1.2, Comments
    • NC-IUBMB, Enzyme Nomenclature, Academic Press, San Diego, 1992, p. 533 (EC 6.5.1.2, Comments).
    • (1992) Enzyme Nomenclature, Academic Press , pp. 533


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.