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Volumn 50, Issue 2, 2005, Pages 69-76

Evaluation of optimal conditions for arginase activity in streptozotocin induced diabetic rats

Author keywords

Arginase; Diabetes; Physicochemical and kinetic properties

Indexed keywords

ARGINASE; ARGININE; MANGANESE; STREPTOZOCIN;

EID: 16244363671     PISSN: 03758427     EISSN: None     Source Type: Journal    
DOI: 10.17221/5598-VETMED     Document Type: Article
Times cited : (13)

References (34)
  • 2
    • 0018907456 scopus 로고
    • The effects of a high fat diet on chronic streptozotocin-diabetic rats
    • Baxter L.C.A., Schofield P.J. (1980): The effects of a high fat diet on chronic streptozotocin-diabetic rats. Diabetologia, 18, 239-245
    • (1980) Diabetologia , vol.18 , pp. 239-245
    • Baxter, L.C.A.1    Schofield, P.J.2
  • 3
    • 0015856930 scopus 로고
    • Effect of manganese and amino acids on proteolytic inactivation of beef liver arginase
    • Bond J.S. (1973): Effect of manganese and amino acids on proteolytic inactivation of beef liver arginase. Biochimica et Biophysica Acta, 327, 157-165
    • (1973) Biochimica et Biophysica Acta , vol.327 , pp. 157-165
    • Bond, J.S.1
  • 4
    • 0020967919 scopus 로고
    • Elevated manganese concentration and arginase activity in livers of streptozotocin-induced diabetic rats
    • Bond J.S., Failla M.L., Unger D.F. (1983): Elevated manganese concentration and arginase activity in livers of streptozotocin-induced diabetic rats. Journal of Biological Chemistry, 258, 8004-8009
    • (1983) Journal of Biological Chemistry , vol.258 , pp. 8004-8009
    • Bond, J.S.1    Failla, M.L.2    Unger, D.F.3
  • 5
    • 0042060112 scopus 로고
    • Properties and regulation of mouse liver arginase
    • In: Schramm V.L., Wedler F.C. (eds.), Academic Press, London and New York
    • Bond J.S., Unger D.F., Garganta C.L. (1986): Properties and regulation of mouse liver arginase. In: Schramm V.L., Wedler F.C. (eds.): Manganese in Metabolism and Enzyme Function. Academic Press, London and New York. 239-257
    • (1986) Manganese in Metabolism and Enzyme Function , pp. 239-257
    • Bond, J.S.1    Unger, D.F.2    Garganta, C.L.3
  • 6
    • 0346313088 scopus 로고    scopus 로고
    • Some properties of purified and non-purified rumen tissue arginase in cattle (in Turkish)
    • Erisir M., Ozan T.S. (1999): Some properties of purified and non-purified rumen tissue arginase in cattle (in Turkish). Turkish Journal of Veterinary and Animal Sciences, 23, 597-608
    • (1999) Turkish Journal of Veterinary and Animal Sciences , vol.23 , pp. 597-608
    • Erisir, M.1    Ozan, T.S.2
  • 7
    • 10144225691 scopus 로고
    • Hormonal regulation of manganese metabolism
    • In: Schramm V.L., Wedler F.C. (eds.), Academic Press, London and New York
    • Failla M.L. (1986): Hormonal regulation of manganese metabolism. In: Schramm V.L., Wedler F.C. (eds.): Manganese in Metabolism and Enzyme Function. Academic Press, London and New York. 93-105
    • (1986) Manganese in Metabolism and Enzyme Function , pp. 93-105
    • Failla, M.L.1
  • 8
    • 0015019510 scopus 로고
    • Rapid method for determination of arginase activity in tissue homogenates
    • Geyer J.W., Dabich D. (1971): Rapid method for determination of arginase activity in tissue homogenates. Analytical Biochemistry, 39, 412-417
    • (1971) Analytical Biochemistry , vol.39 , pp. 412-417
    • Geyer, J.W.1    Dabich, D.2
  • 9
    • 0015864404 scopus 로고
    • Arginase isozymes of rat mammary gland, liver, and other tissues
    • Glass R.D., Knox W.E. (1973): Arginase isozymes of rat mammary gland, liver, and other tissues. Journal of Biological Chemistry, 248, 5785-5789
    • (1973) Journal of Biological Chemistry , vol.248 , pp. 5785-5789
    • Glass, R.D.1    Knox, W.E.2
  • 10
    • 78651135141 scopus 로고
    • Protein catabolism and protein synthesis in perfused livers of normal and alloxan-diabetic rats
    • Green M., Miller L.L. (1960): Protein catabolism and protein synthesis in perfused livers of normal and alloxan-diabetic rats. Journal of Biological Chemistry, 235, 3202-3208
    • (1960) Journal of Biological Chemistry , vol.235 , pp. 3202-3208
    • Green, M.1    Miller, L.L.2
  • 12
    • 0020698984 scopus 로고
    • Regulation expression of genes for enzymes of the mammalian urea cycle in permanent cell-culture lines of hepatic and non-hepatic origin
    • Haggerty D.F., Spector E.B., Lynch M., Kern R., Frank L.B., Cederbaum S.D. (1983): Regulation expression of genes for enzymes of the mammalian urea cycle in permanent cell-culture lines of hepatic and non-hepatic origin. Molecular and Cellular Biochemistry, 53/54, 57-76
    • (1983) Molecular and Cellular Biochemistry , vol.53 , Issue.54 , pp. 57-76
    • Haggerty, D.F.1    Spector, E.B.2    Lynch, M.3    Kern, R.4    Frank, L.B.5    Cederbaum, S.D.6
  • 13
    • 0015238976 scopus 로고
    • Nuclear magnetic resonance studies of manganese binding of rat liver arginase
    • Hirsch-Kolb H., Kolb H.J., Greenberg D.M. (1971): Nuclear magnetic resonance studies of manganese binding of rat liver arginase. Journal of Biological Chemistry, 246, 395-401
    • (1971) Journal of Biological Chemistry , vol.246 , pp. 395-401
    • Hirsch-Kolb, H.1    Kolb, H.J.2    Greenberg, D.M.3
  • 14
    • 0023631866 scopus 로고
    • Induction of the five urea-cycle enzymes by glucagon in cultured foetal rat hepatocytes
    • Husson A., Buquet C., Vaillant R. (1987): Induction of the five urea-cycle enzymes by glucagon in cultured foetal rat hepatocytes. Differentiation, 35, 212-218
    • (1987) Differentiation , vol.35 , pp. 212-218
    • Husson, A.1    Buquet, C.2    Vaillant, R.3
  • 16
    • 0019845128 scopus 로고
    • Changes in the levels of urea cycle enzymes and in metabolites thereof in diabetes
    • Jorda A., Cabo J., Grisolia S. (1981): Changes in the levels of urea cycle enzymes and in metabolites thereof in diabetes. Enzyme, 26, 240-244
    • (1981) Enzyme , vol.26 , pp. 240-244
    • Jorda, A.1    Cabo, J.2    Grisolia, S.3
  • 19
    • 0015656354 scopus 로고
    • Purification and properties of arginase of rat kidney
    • Kaysen G.A., Strecker H.J. (1973): Purification and properties of arginase of rat kidney. Biochemical Journal, 133, 779-788
    • (1973) Biochemical Journal , vol.133 , pp. 779-788
    • Kaysen, G.A.1    Strecker, H.J.2
  • 20
    • 0016574771 scopus 로고
    • Studies on L-arginase the small intestine
    • Konarska L., Tomaszewski L. (1975): Studies on L-arginase the small intestine. Biochemical Medicine, 14, 250-262
    • (1975) Biochemical Medicine , vol.14 , pp. 250-262
    • Konarska, L.1    Tomaszewski, L.2
  • 22
    • 0038237410 scopus 로고
    • Influence of pancreatic hormones on enzymes concerned with urea synthesis in rat liver
    • McLean P., Novello F. (1965): Influence of pancreatic hormones on enzymes concerned with urea synthesis in rat liver. Biochemical Journal, 94, 410-422
    • (1965) Biochemical Journal , vol.94 , pp. 410-422
    • McLean, P.1    Novello, F.2
  • 24
    • 0344806998 scopus 로고
    • Urea synthesis and ammonia metabolism
    • In: Arias I., Popper H., Schachter D., Shafrits D.A. (eds.), Raven Press, New York
    • Powers G.S., Meister T. (1982): Urea synthesis and ammonia metabolism. In: Arias I., Popper H., Schachter D., Shafrits D.A. (eds.): The Liver: Biology and Pathobiology. Raven Press, New York. 251-263
    • (1982) The Liver: Biology and Pathobiology , pp. 251-263
    • Powers, G.S.1    Meister, T.2
  • 25
    • 0028085936 scopus 로고
    • Rat liver arginase: kinetic mechanism, alternate substrates, and inhibitors
    • Reczkowski R.S., Ash D.E. (1994): Rat liver arginase: kinetic mechanism, alternate substrates, and inhibitors. Archives of Biochemistry and Biophysics, 312, 31-37
    • (1994) Archives of Biochemistry and Biophysics , vol.312 , pp. 31-37
    • Reczkowski, R.S.1    Ash, D.E.2
  • 26
    • 10544224144 scopus 로고    scopus 로고
    • Effects of vanadate and insulin on the activities of selected enzymes of amino acid metabolism in alloxan diabetic rat kidney
    • Upadhyaya S.K.C., Baquer N.Z. (1996): Effects of vanadate and insulin on the activities of selected enzymes of amino acid metabolism in alloxan diabetic rat kidney. Biochemistry and Molecular Biology International, 40, 853-860
    • (1996) Biochemistry and Molecular Biology International , vol.40 , pp. 853-860
    • Upadhyaya, S.K.C.1    Baquer, N.Z.2
  • 27
    • 0033114785 scopus 로고    scopus 로고
    • Modulation of mRNA levels of liver arginase by insulin and vanadate in experimental diabetes
    • Upadhyaya S.K.C., Raju J., Baquer N.Z. (1999): Modulation of mRNA levels of liver arginase by insulin and vanadate in experimental diabetes. Indian Journal of Biochemistry and Biophysics, 36, 125-128
    • (1999) Indian Journal of Biochemistry and Biophysics , vol.36 , pp. 125-128
    • Upadhyaya, S.K.C.1    Raju, J.2    Baquer, N.Z.3
  • 28
    • 84961050939 scopus 로고
    • Adaptive characteristics of urea cycle enzymes in the rat
    • Schimke R.T. (1962): Adaptive characteristics of urea cycle enzymes in the rat. Journal of Biological Chemistry, 237, 459-468
    • (1962) Journal of Biological Chemistry , vol.237 , pp. 459-468
    • Schimke, R.T.1
  • 29
    • 0030848844 scopus 로고    scopus 로고
    • Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function
    • Scolnick L.R., Kanyo Z.F., Cavalli R.C., Ash D.E., Christianson D.W. (1997): Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function. Biochemistry, 36, 10558-10565
    • (1997) Biochemistry , vol.36 , pp. 10558-10565
    • Scolnick, L.R.1    Kanyo, Z.F.2    Cavalli, R.C.3    Ash, D.E.4    Christianson, D.W.5
  • 31
    • 0024439993 scopus 로고
    • Comparison of biochemical properties of liver arginase from streptozocin-induced diabetic and control mice
    • Spolarics Z., Bond J.S. (1989): Comparison of biochemical properties of liver arginase from streptozocin-induced diabetic and control mice. Archives of Biochemistry and Biophysics, 274, 426-433
    • (1989) Archives of Biochemistry and Biophysics , vol.274 , pp. 426-433
    • Spolarics, Z.1    Bond, J.S.2
  • 34
    • 0023575388 scopus 로고
    • Does a common mechanism induce the diverse complications of diabetes?
    • Winegrad A.I. (1987): Does a common mechanism induce the diverse complications of diabetes? Diabetes, 36, 396-406
    • (1987) Diabetes , vol.36 , pp. 396-406
    • Winegrad, A.I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.