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Volumn 29, Issue 7, 1997, Pages 985-992

Characterization of multiple acid phosphatases in bovine liver cytosol and lysosome. Inactivation of cytosolic enzymes by disulfides and its redox regulation by thioltransferase

Author keywords

Acid phosphatase; Cytosol; Lysosome; Multiple forms; Oxidative stress

Indexed keywords

ACID PHOSPHATASE;

EID: 0030724144     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(97)00044-7     Document Type: Article
Times cited : (10)

References (32)
  • 1
    • 0014312009 scopus 로고
    • Evidence for a substrate-mediated change in conformation of rabbit muscle aldolase
    • Adelman R. C., Morse D. E. and Horecker B. L. (1968) Evidence for a substrate-mediated change in conformation of rabbit muscle aldolase. Archives in Biochemistry and Biophysics 126, 343-352.
    • (1968) Archives in Biochemistry and Biophysics , vol.126 , pp. 343-352
    • Adelman, R.C.1    Morse, D.E.2    Horecker, B.L.3
  • 2
    • 0021104499 scopus 로고
    • New assay for enzymatic phosphate release: Application to aspartate transcarbamylase and other enzymes
    • Bencini D. A., Shanley M. S., Wild J. R. and O'Donovan G. A. (1983) New assay for enzymatic phosphate release: application to aspartate transcarbamylase and other enzymes. Analytical Biochemistry 132, 259-264.
    • (1983) Analytical Biochemistry , vol.132 , pp. 259-264
    • Bencini, D.A.1    Shanley, M.S.2    Wild, J.R.3    O'Donovan, G.A.4
  • 5
    • 0024008325 scopus 로고
    • Evidence of acid phosphatase in the cytoplasma as a distinct entity
    • Chen C.-H. and Chen S. C. (1988) Evidence of acid phosphatase in the cytoplasma as a distinct entity. Archives in Biochemistry and Biophysics 262, 427-438.
    • (1988) Archives in Biochemistry and Biophysics , vol.262 , pp. 427-438
    • Chen, C.-H.1    Chen, S.C.2
  • 6
    • 0018800304 scopus 로고
    • + -dependent glyceraldehyde 3-phosphate dehydrogenases from Streptococcus mutants
    • + -dependent glyceraldehyde 3-phosphate dehydrogenases from Streptococcus mutants. Journal of Biological Chemistry 254, 1134-1142.
    • (1979) Journal of Biological Chemistry , vol.254 , pp. 1134-1142
    • Crow, V.L.1    Wittenberger, C.L.2
  • 7
    • 0028363734 scopus 로고
    • Kinetic and site-directed mutagenesis studies of the cysteine residues of bovine low molecular weight phosphotyrosyl protein phosphatase
    • Davis J. P., Zhou M.-M. and van Etten R. L. (1994) Kinetic and site-directed mutagenesis studies of the cysteine residues of bovine low molecular weight phosphotyrosyl protein phosphatase. Journal of Biological Chemistry 269, 8734-8740.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 8734-8740
    • Davis, J.P.1    Zhou, M.-M.2    Van Etten, R.L.3
  • 8
    • 0025909426 scopus 로고
    • Purple acid phosphatase from bovine spleen. Interaction at the active site in relation to the reaction mechanism
    • Dietrich M., Muenstermann D., Suerbaum H. and Witzel H. (1991) Purple acid phosphatase from bovine spleen. Interaction at the active site in relation to the reaction mechanism. European Journal of Biochemistry 199, 105-113.
    • (1991) European Journal of Biochemistry , vol.199 , pp. 105-113
    • Dietrich, M.1    Muenstermann, D.2    Suerbaum, H.3    Witzel, H.4
  • 9
    • 0014216842 scopus 로고
    • Separation and properties of three acid phosphatases from human placenta
    • Dipietro D. L. and Zenglerle F. S. (1967) Separation and properties of three acid phosphatases from human placenta. Journal of Biological Chemistry 242, 3391-3396.
    • (1967) Journal of Biological Chemistry , vol.242 , pp. 3391-3396
    • Dipietro, D.L.1    Zenglerle, F.S.2
  • 11
    • 0014689995 scopus 로고
    • Purification and characterization of a low molecular weight acid phosphatase from bovine liver
    • Heinrikson R. L. (1969) Purification and characterization of a low molecular weight acid phosphatase from bovine liver. Journal of Biological Chemistry 244, 299-307.
    • (1969) Journal of Biological Chemistry , vol.244 , pp. 299-307
    • Heinrikson, R.L.1
  • 12
    • 0019874676 scopus 로고
    • Comparative inactivation and inhibition of the anomerase and isomerase activities of phosphoglucose isomerase
    • Howell E. E. and Schray K. J. (1981) Comparative inactivation and inhibition of the anomerase and isomerase activities of phosphoglucose isomerase. Molecular and Cell Biochemistry 37, 101-107.
    • (1981) Molecular and Cell Biochemistry , vol.37 , pp. 101-107
    • Howell, E.E.1    Schray, K.J.2
  • 14
    • 0015523085 scopus 로고
    • Regulation of aspartate aminotransferase isozymes by d-erythrose 4-phosphate and glycoaldehyde phosphate, naturally occuring homologues of d-glyceraldehyde 3-phosphate
    • Kopelvich L., Sweetman L. and Nisselbaum J. S. (1972) Regulation of aspartate aminotransferase isozymes by D-erythrose 4-phosphate and glycoaldehyde phosphate, naturally occuring homologues of D-glyceraldehyde 3-phosphate. Journal of Biological Chemistry 247, 273-287.
    • (1972) Journal of Biological Chemistry , vol.247 , pp. 273-287
    • Kopelvich, L.1    Sweetman, L.2    Nisselbaum, J.S.3
  • 15
    • 0019448453 scopus 로고
    • The low-molecular-weight acid phosphatase from bovine liver: Isolation, amino acid composition, and chemical modification studies
    • Lawrence G. L. and van Etten R. L. (1981) The low-molecular-weight acid phosphatase from bovine liver: isolation, amino acid composition, and chemical modification studies. Archives in Biochemistry and Biophysics 206, 122-131.
    • (1981) Archives in Biochemistry and Biophysics , vol.206 , pp. 122-131
    • Lawrence, G.L.1    Van Etten, R.L.2
  • 16
  • 17
    • 0029164326 scopus 로고
    • The role of cysteine in the alteration of bovine liver dihydrodiol dehydrogenase 3 activity
    • Nanjo H., Adachi H., Aketa M., Mizoguchi T., Nishihara T. and Terada T. (1995) The role of cysteine in the alteration of bovine liver dihydrodiol dehydrogenase 3 activity. Biochemical Journal 310, 101-107.
    • (1995) Biochemical Journal , vol.310 , pp. 101-107
    • Nanjo, H.1    Adachi, H.2    Aketa, M.3    Mizoguchi, T.4    Nishihara, T.5    Terada, T.6
  • 19
    • 0027499031 scopus 로고
    • Difference in glutathione S-transferase response to oxidative stress between porcine and bovine lens
    • Nishinaka T., Terada T., Nanjo H., Mizoguchi T. and Nishihara T. (1993) Difference in glutathione S-transferase response to oxidative stress between porcine and bovine lens. Experimental Eye Research 56, 299-303.
    • (1993) Experimental Eye Research , vol.56 , pp. 299-303
    • Nishinaka, T.1    Terada, T.2    Nanjo, H.3    Mizoguchi, T.4    Nishihara, T.5
  • 20
    • 0022368071 scopus 로고
    • Two isoenzymes of chicken muscle acylphosphatase: Purification and properties
    • Ohba Y., Mizuo Y., Takasawa T. and Shiokawa H. (1985) Two isoenzymes of chicken muscle acylphosphatase: purification and properties. Journal of Biochemistry (Tokyo) 98, 909-919.
    • (1985) Journal of Biochemistry (Tokyo) , vol.98 , pp. 909-919
    • Ohba, Y.1    Mizuo, Y.2    Takasawa, T.3    Shiokawa, H.4
  • 22
    • 0024361299 scopus 로고
    • The 18 kDa cytosolic acid phosphatase from bovine live has phosphotyrosine phosphatase activity on the autophosphorylated epidermal growth factor receptor
    • Ramponi G., Manao G., Camici G., Cappugi G., Ruggiero M. and Bottaro D. P. (1989) The 18 kDa cytosolic acid phosphatase from bovine live has phosphotyrosine phosphatase activity on the autophosphorylated epidermal growth factor receptor. FEBS Letters 250, 2, 469-473.
    • (1989) FEBS Letters , vol.250 , Issue.2 , pp. 469-473
    • Ramponi, G.1    Manao, G.2    Camici, G.3    Cappugi, G.4    Ruggiero, M.5    Bottaro, D.P.6
  • 23
    • 50549210626 scopus 로고
    • Acid phosphatase of the lysosomal and soluble fraction of rat liver
    • Shibka S. and Tappel A. L. (1963) Acid phosphatase of the lysosomal and soluble fraction of rat liver. Biochimica et Biophysica Acta 73, 76-86.
    • (1963) Biochimica et Biophysica Acta , vol.73 , pp. 76-86
    • Shibka, S.1    Tappel, A.L.2
  • 25
    • 0027996676 scopus 로고
    • Thioltransferase can utilize as same as glutathione as a reductant during the restoration of cystamine-treated glucose 6-phosphate dehydrogenase activity
    • Terada T. (1994) Thioltransferase can utilize as same as glutathione as a reductant during the restoration of cystamine-treated glucose 6-phosphate dehydrogenase activity. Biochemistry and Molecular Biology International 34, 723-727.
    • (1994) Biochemistry and Molecular Biology International , vol.34 , pp. 723-727
    • Terada, T.1
  • 26
    • 0021952795 scopus 로고
    • Purification and properties of beef liver aldehyde reductase catalyzing the reduction of d-erythrose 4-phosphate
    • Terada T., Kohno T., Samejima T., Hosomi S., Mizoguchi T. and Uehara K. (1985a) Purification and properties of beef liver aldehyde reductase catalyzing the reduction of D-erythrose 4-phosphate. Journal of Biochemistry (Tokyo) 97, 79-87.
    • (1985) Journal of Biochemistry (Tokyo) , vol.97 , pp. 79-87
    • Terada, T.1    Kohno, T.2    Samejima, T.3    Hosomi, S.4    Mizoguchi, T.5    Uehara, K.6
  • 27
  • 28
    • 0022425866 scopus 로고
    • Characterization of an enzyme which catalyses isomerization and epimerization of d-erythrose 4-phosphate
    • Terada T., Mukae H.. Ohashi K., Hosomi S., Mizoguchi T. and Uehara K. (1985b) Characterization of an enzyme which catalyses isomerization and epimerization of D-erythrose 4-phosphate. European Journal of Biochemistry 148, 345-351.
    • (1985) European Journal of Biochemistry , vol.148 , pp. 345-351
    • Terada, T.1    Mukae, H.2    Ohashi, K.3    Hosomi, S.4    Mizoguchi, T.5    Uehara, K.6
  • 30
    • 0016367419 scopus 로고
    • Studies on d-tetrose metabolism. IV. Purification and properties of d-erythrulose reductase from beef liver
    • Uehara K., Tanimoto T. and Sato H. (1974) Studies on D-tetrose metabolism. IV. Purification and properties of D-erythrulose reductase from beef liver. Journal of Biochemistry (Tokyo) 75, 333-345.
    • (1974) Journal of Biochemistry (Tokyo) , vol.75 , pp. 333-345
    • Uehara, K.1    Tanimoto, T.2    Sato, H.3
  • 31
    • 0024995069 scopus 로고
    • Purification and characterization of a low-molecular weight acid phosphatase - A phosphotyrosyl-protein phosphatases from bovine heart
    • Zhang Z.-Y. and van Etten R. L. (1990) Purification and characterization of a low-molecular weight acid phosphatase - a phosphotyrosyl-protein phosphatases from bovine heart. Archives in Biochemistry and Biophysics 282, 39-49.
    • (1990) Archives in Biochemistry and Biophysics , vol.282 , pp. 39-49
    • Zhang, Z.-Y.1    Van Etten, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.