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Volumn 45, Issue 10, 1997, Pages 1427-1431

Kinetic parameters of lactate dehydrogenase in liver and gastrocnemius determined by three quantitative histochemical methods

Author keywords

Enzyme kinetics; Image analysis; Lactate dehydrogenase; Liver; Maximal reaction velocities; Michaelis constants; Quantitative histochemistry; Skeletal muscle

Indexed keywords

ANIMAL CELL; ARTICLE; ENZYME ACTIVITY; ENZYME MECHANISM; GASTROCNEMIUS MUSCLE; HISTOCHEMISTRY; MICHAELIS CONSTANT; MOUSE; MUSCLE CELL; NONHUMAN; PRIORITY JOURNAL; RABBIT;

EID: 0030826429     PISSN: 00221554     EISSN: None     Source Type: Journal    
DOI: 10.1177/002215549704501011     Document Type: Article
Times cited : (11)

References (31)
  • 1
    • 0014804006 scopus 로고
    • Catalytic properties of the lactate dehydrogenase isozyme "X" from mouse testis
    • Battellino LJ, Blanco A ( 1970) Catalytic properties of the lactate dehydrogenase isozyme "X" from mouse testis. J Exp Zool 174: 173-186
    • (1970) J Exp Zool , vol.174 , pp. 173-186
    • Battellino, L.J.1    Blanco, A.2
  • 2
    • 0014409906 scopus 로고
    • Kinetic properties of rabbit testicular lactate dehydrogenase isozyme
    • Battellino LJ, Jaime FR, Blanco A (1968) Kinetic properties of rabbit testicular lactate dehydrogenase isozyme. J Biol Chem 243: 5185-5192
    • (1968) J Biol Chem , vol.243 , pp. 5185-5192
    • Battellino, L.J.1    Jaime, F.R.2    Blanco, A.3
  • 3
    • 0015817965 scopus 로고
    • The kinetics of the interconversion of intermediates of the reaction of pig muscle lactate dehydrogenase with oxidized nicotinamide-adenine dinucleotide and lactate
    • Bennett NG, Gutfreund H (1973) The kinetics of the interconversion of intermediates of the reaction of pig muscle lactate dehydrogenase with oxidized nicotinamide-adenine dinucleotide and lactate. Biochem J 135:81-85
    • (1973) Biochem J , vol.135 , pp. 81-85
    • Bennett, N.G.1    Gutfreund, H.2
  • 4
    • 0014766330 scopus 로고
    • Studies on succinate oxidation. I. The use of intact tissue sections
    • Butcher RG (1970) Studies on succinate oxidation. I. The use of intact tissue sections. Exp Cell Res 60:54-60
    • (1970) Exp Cell Res , vol.60 , pp. 54-60
    • Butcher, R.G.1
  • 5
    • 0018069303 scopus 로고
    • The measurement in tissue sections of the two formazans derived from nitroblue tetrazolium in dehydrogenase reactions
    • Butcher RG (1978) The measurement in tissue sections of the two formazans derived from nitroblue tetrazolium in dehydrogenase reactions. Histochem J 10:739-744
    • (1978) Histochem J , vol.10 , pp. 739-744
    • Butcher, R.G.1
  • 6
    • 0002631790 scopus 로고
    • Glycolytic enzyme organization via the cytoskeleton and its role in metabolic regulation
    • Beitner R, ed. Boca Raton, FL, CRC Press
    • Clarke F, Stephan P, Morton D, Weidemann J (1985) Glycolytic enzyme organization via the cytoskeleton and its role in metabolic regulation. In Beitner R, ed. Regulation of Carbohydrate Metabolism. Boca Raton, FL, CRC Press, 1-31
    • (1985) Regulation of Carbohydrate Metabolism , pp. 1-31
    • Clarke, F.1    Stephan, P.2    Morton, D.3    Weidemann, J.4
  • 7
    • 0016670453 scopus 로고
    • Immunofluorescent localization of glycogenolytic and glycolytic enzyme proteins and of malate dehydrogenase isozymes in cross-striated skeletal muscle and heart of the rabbit
    • Dölken G, Leisner E, Pette D (1975) Immunofluorescent localization of glycogenolytic and glycolytic enzyme proteins and of malate dehydrogenase isozymes in cross-striated skeletal muscle and heart of the rabbit. Histochemistry 43:113-121
    • (1975) Histochemistry , vol.43 , pp. 113-121
    • Dölken, G.1    Leisner, E.2    Pette, D.3
  • 8
    • 0028200686 scopus 로고
    • A quantitative histochemical study of xanthine oxidase activity in rat liver using the cerium capture method in the presence of polyvinyl alcohol
    • Frederiks WM, Bosch KS, Van Den Munckhof RJM, Van Noorden CJF (1994) A quantitative histochemical study of xanthine oxidase activity in rat liver using the cerium capture method in the presence of polyvinyl alcohol. J Histochem Cytochem 42:1091-1096
    • (1994) J Histochem Cytochem , vol.42 , pp. 1091-1096
    • Frederiks, W.M.1    Bosch, K.S.2    Van Den Munckhof, R.J.M.3    Van Noorden, C.J.F.4
  • 10
    • 0024421740 scopus 로고
    • In situ kinetic parameters of glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase in different areas of the rat liver acinus
    • Jonges GN, Van Noorden CJF (1989) In situ kinetic parameters of glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase in different areas of the rat liver acinus. Histochem J 21:585-594
    • (1989) Histochem J , vol.21 , pp. 585-594
    • Jonges, G.N.1    Van Noorden, C.J.F.2
  • 11
    • 0023669162 scopus 로고
    • Demonstration of tubulin-glycolytic enzyme interactions using a novel electrophoretic approach
    • Karkhoff-Schweizer R, Knull HR (1987) Demonstration of tubulin-glycolytic enzyme interactions using a novel electrophoretic approach. Biochem Biophys Res Commun 146:827-831
    • (1987) Biochem Biophys Res Commun , vol.146 , pp. 827-831
    • Karkhoff-Schweizer, R.1    Knull, H.R.2
  • 13
    • 0027962614 scopus 로고
    • Effect of tubulin on the activity of the muscle isoenzyme of lactate dehydrogenase
    • Marmillot P, Keith T, Srivastava DK, Knull HR (1994) Effect of tubulin on the activity of the muscle isoenzyme of lactate dehydrogenase. Arch Biochem Biophys 315:467-472
    • (1994) Arch Biochem Biophys , vol.315 , pp. 467-472
    • Marmillot, P.1    Keith, T.2    Srivastava, D.K.3    Knull, H.R.4
  • 14
    • 0027528589 scopus 로고
    • Estimating the initial reaction velocity of a soluble dehydrogenase in situ
    • Nakae Y, Stoward PJ (1993a) Estimating the initial reaction velocity of a soluble dehydrogenase in situ. Histochem J 25:199-205
    • (1993) Histochem J , vol.25 , pp. 199-205
    • Nakae, Y.1    Stoward, P.J.2
  • 15
    • 0027405164 scopus 로고
    • Kinetic analysis of lactate dehydrogenase in situ in mouse liver determined with a quantitative histochemical technique
    • Nakae Y, Stoward PJ (1993b) Kinetic analysis of lactate dehydrogenase in situ in mouse liver determined with a quantitative histochemical technique. Histochem J 25:206-212
    • (1993) Histochem J , vol.25 , pp. 206-212
    • Nakae, Y.1    Stoward, P.J.2
  • 16
    • 0028203542 scopus 로고
    • The initial reaction velocities of lactate dehydrogenase in various cell types
    • Nakae Y, Stoward PJ (1994a) The initial reaction velocities of lactate dehydrogenase in various cell types. Histochem J 26:283-291
    • (1994) Histochem J , vol.26 , pp. 283-291
    • Nakae, Y.1    Stoward, P.J.2
  • 17
    • 0028345689 scopus 로고
    • The diverse Michaelis constants and maximum velocities of lactate dehydrogenase in situ in various types of cell
    • Nakae Y, Stoward PJ (1994b) The diverse Michaelis constants and maximum velocities of lactate dehydrogenase in situ in various types of cell. Histochem J 26:292-297
    • (1994) Histochem J , vol.26 , pp. 292-297
    • Nakae, Y.1    Stoward, P.J.2
  • 18
    • 0030764273 scopus 로고    scopus 로고
    • The effects of tissue protectants on the kinetics of lactate dehydrogenase within cells
    • Nakae Y, Stoward PJ (1997) The effects of tissue protectants on the kinetics of lactate dehydrogenase within cells. J Histochem Cytochem 45:1417-1425
    • (1997) J Histochem Cytochem , vol.45 , pp. 1417-1425
    • Nakae, Y.1    Stoward, P.J.2
  • 19
    • 7344232398 scopus 로고
    • Purification, kinetic, and immunochemical studies of the major variants of lactic dehydrogenase from human liver, hepatoma, and erythrocytes; comparison with the major variant of human heart lactic dehydrogenase
    • Nisselbaum JS, Bodansky O (1963) Purification, kinetic, and immunochemical studies of the major variants of lactic dehydrogenase from human liver, hepatoma, and erythrocytes; comparison with the major variant of human heart lactic dehydrogenase. J Biol Chem 238:969-974
    • (1963) J Biol Chem , vol.238 , pp. 969-974
    • Nisselbaum, J.S.1    Bodansky, O.2
  • 20
    • 15444342568 scopus 로고
    • Comparison of the actions of human brain, liver, and heart lactic dehydrogenase variants on nucleotide analogues and on substrate analogues in the absence and in the presence of oxalate and oxamate
    • Nisselhaum JS, Packer DE, Bodansky O (1964) Comparison of the actions of human brain, liver, and heart lactic dehydrogenase variants on nucleotide analogues and on substrate analogues in the absence and in the presence of oxalate and oxamate. J Biol Chem 239:2830-2834
    • (1964) J Biol Chem , vol.239 , pp. 2830-2834
    • Nisselhaum, J.S.1    Packer, D.E.2    Bodansky, O.3
  • 21
    • 0017074822 scopus 로고
    • A comparison of some kinetic properties of soluble and bound lactate dehydrogenase isoenzymes at different temperatures
    • Nitisewojo P, Hultin HO (1976) A comparison of some kinetic properties of soluble and bound lactate dehydrogenase isoenzymes at different temperatures. Eur J Biochem 67:87-94
    • (1976) Eur J Biochem , vol.67 , pp. 87-94
    • Nitisewojo, P.1    Hultin, H.O.2
  • 22
    • 0000532545 scopus 로고
    • The comparative enzymology of lactic dehydrogenases. I. Properties of the crystalline beef and chicken enzymes
    • Pesce A, McKay RH, Stolzenbach F, Cahn RD, Kaplan NO (1964) The comparative enzymology of lactic dehydrogenases. I. Properties of the crystalline beef and chicken enzymes. J Biol Chem 239:1753-1761
    • (1964) J Biol Chem , vol.239 , pp. 1753-1761
    • Pesce, A.1    McKay, R.H.2    Stolzenbach, F.3    Cahn, R.D.4    Kaplan, N.O.5
  • 23
    • 0022961292 scopus 로고
    • Interaction of actin with the enzymes of carbohydrate metabolism
    • Poglazov BF, Livanova NB (1986) Interaction of actin with the enzymes of carbohydrate metabolism. Adv Enzyme Regul 25:297-305
    • (1986) Adv Enzyme Regul , vol.25 , pp. 297-305
    • Poglazov, B.F.1    Livanova, N.B.2
  • 24
    • 0020327611 scopus 로고
    • 20α-hydroxysteroid dehydrogenase activity in the rat corpus luteum; a quantitative cytochemical study
    • Robertson WR, Frost J, Hoyer PE, Weinkove C (1982) 20α-hydroxysteroid dehydrogenase activity in the rat corpus luteum; a quantitative cytochemical study. J Steroid Biochem 17:237-243
    • (1982) J Steroid Biochem , vol.17 , pp. 237-243
    • Robertson, W.R.1    Frost, J.2    Hoyer, P.E.3    Weinkove, C.4
  • 25
    • 0020827140 scopus 로고
    • Histochemical localization and quantification of glucose-6-phosphate dehydrogenase in bovine Leydig cells
    • Sinowatz F, Scheubeck M, Wrobel K-H, Zwack M (1983) Histochemical localization and quantification of glucose-6-phosphate dehydrogenase in bovine Leydig cells. Histochem J 15: 831-844
    • (1983) Histochem J , vol.15 , pp. 831-844
    • Sinowatz, F.1    Scheubeck, M.2    Wrobel, K.-H.3    Zwack, M.4
  • 27
    • 0022743296 scopus 로고
    • A quantitative histochemical study of NADPH-ferrihemoprotein reductase activity
    • Van Noorden CJF, Butcher RG (1986) A quantitative histochemical study of NADPH-ferrihemoprotein reductase activity. Histochem J 18:364-370
    • (1986) Histochem J , vol.18 , pp. 364-370
    • Van Noorden, C.J.F.1    Butcher, R.G.2
  • 28
    • 0023127147 scopus 로고
    • Quantification of the histochemical reaction for alkaline phosphatase activity using the indoxyl-tetranitro BT method
    • Van Noorden CJF, Jonges GN (1987) Quantification of the histochemical reaction for alkaline phosphatase activity using the indoxyl-tetranitro BT method. Histochem J 19:94-102
    • (1987) Histochem J , vol.19 , pp. 94-102
    • Van Noorden, C.J.F.1    Jonges, G.N.2
  • 29
    • 84954160919 scopus 로고
    • Assessment of immunocytochemical techniques with particular reference to the mixed-aggregation immunocytochemical technique
    • Evered D, O'Connor M, eds. Amsterdam, Excerpta Medica
    • Wachsmuth ED (1980) Assessment of immunocytochemical techniques with particular reference to the mixed-aggregation immunocytochemical technique. In Evered D, O'Connor M, eds. Trends in Enzyme Histochemistry and Cytochemistry: Ciba Foundation Symposium 73 (new ser.). Amsterdam, Excerpta Medica, 135-153
    • (1980) Trends in Enzyme Histochemistry and Cytochemistry: Ciba Foundation Symposium 73 (New Ser.) , pp. 135-153
    • Wachsmuth, E.D.1
  • 30
    • 0024342987 scopus 로고
    • Glycolytic enzyme interactions with tubulin and microtubules
    • Walsh JL, Keith TJ, Knull HR (1989) Glycolytic enzyme interactions with tubulin and microtubules. Biochim Biophys Acta 999:64-70
    • (1989) Biochim Biophys Acta , vol.999 , pp. 64-70
    • Walsh, J.L.1    Keith, T.J.2    Knull, H.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.