메뉴 건너뛰기




Volumn 110, Issue 3, 1998, Pages 243-250

Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: Confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis

Author keywords

[No Author keywords available]

Indexed keywords

3 MERCAPTOPYRUVATE SULFURTRANSFERASE; F ACTIN; FLUORESCEIN ISOTHIOCYANATE; ISOTHIOCYANIC ACID DERIVATIVE; MITOCHONDRIAL ENZYME; PHALLOIDIN; SULFURTRANSFERASE; THIOSULFATE SULFURTRANSFERASE; UNCLASSIFIED DRUG;

EID: 0031666759     PISSN: 09486143     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004180050286     Document Type: Article
Times cited : (188)

References (30)
  • 1
    • 0024599146 scopus 로고
    • Comparative studies on the distribution of rhodanese and β-mercaptopyruvate sulfurtransferase in different organs of sheep and cattle
    • Aminlari M, Gilanpour H, Taghavianpour H, Veseghi T (1989) Comparative studies on the distribution of rhodanese and β-mercaptopyruvate sulfurtransferase in different organs of sheep and cattle. Comp Biochem Physiol 92c:259-262
    • (1989) Comp Biochem Physiol , vol.92 C , pp. 259-262
    • Aminlari, M.1    Gilanpour, H.2    Taghavianpour, H.3    Veseghi, T.4
  • 2
    • 77049229661 scopus 로고
    • Tissue fractionation studies. Intracellular distribution patterns of enzymes in rat liver tissue
    • Duve C, Pressman BC, Gianetto R, Wattiaux R, Appelmans F (1955) Tissue fractionation studies. Intracellular distribution patterns of enzymes in rat liver tissue. Biochem J 60:604-617
    • (1955) Biochem J , vol.60 , pp. 604-617
    • Duve, C.1    Pressman, B.C.2    Gianetto, R.3    Wattiaux, R.4    Appelmans, F.5
  • 3
    • 0006688735 scopus 로고
    • A possible role for rhodanese: The formation of "labile" sulphur from thiosulphate
    • FinazziArgò A, Canella C, Grazizni MT, Cavallini D (1971) A possible role for rhodanese: the formation of "labile" sulphur from thiosulphate. FEBS Lett 16:172-174
    • (1971) FEBS Lett , vol.16 , pp. 172-174
    • FinazziArgò, A.1    Canella, C.2    Grazizni, M.T.3    Cavallini, D.4
  • 5
    • 0028068519 scopus 로고
    • Structure of the sequences for two mitochondrial matrix proteins that are not proteolytically processed upon import
    • Hammen PK, Gorenstein DG, Weiner H (1994) Structure of the sequences for two mitochondrial matrix proteins that are not proteolytically processed upon import. Biochemistry 33:8610-8617
    • (1994) Biochemistry , vol.33 , pp. 8610-8617
    • Hammen, P.K.1    Gorenstein, D.G.2    Weiner, H.3
  • 6
    • 0026695884 scopus 로고
    • Subcellular localization of xanthine oxidase in rat hepatocytes: High-resolution immunoelectron microscopic study combined with biochemical analysis
    • Ichikuwa M, Nishino T, Nishino T, Ichikawa A (1992) Subcellular localization of xanthine oxidase in rat hepatocytes: high-resolution immunoelectron microscopic study combined with biochemical analysis. J Histochem Cytochem 40:1097-1103
    • (1992) J Histochem Cytochem , vol.40 , pp. 1097-1103
    • Ichikuwa, M.1    Nishino, T.2    Nishino, T.3    Ichikawa, A.4
  • 7
    • 0017883472 scopus 로고
    • Steady-state kinetics of 3-mercaptopyruvate sulfurtransferase from bovine kidney
    • Jarabak R, Westley J (1978) Steady-state kinetics of 3-mercaptopyruvate sulfurtransferase from bovine kidney. Arch Biochem Biophys 185:458-465
    • (1978) Arch Biochem Biophys , vol.185 , pp. 458-465
    • Jarabak, R.1    Westley, J.2
  • 8
    • 0014234438 scopus 로고
    • Enzymic reduction of thiosulphate in preparations from beef liver
    • Koj A (1968) Enzymic reduction of thiosulphate in preparations from beef liver. Acta Biochim Pol 15:161-169
    • (1968) Acta Biochim Pol , vol.15 , pp. 161-169
    • Koj, A.1
  • 9
    • 0016718909 scopus 로고
    • Subcellular distribution and intramitochondrial localization of the three sulfurtransferases in rat liver
    • Koj A, Frendo J, Wojtczak L (1975) Subcellular distribution and intramitochondrial localization of the three sulfurtransferases in rat liver. FEBS Lett 57:42-46
    • (1975) FEBS Lett , vol.57 , pp. 42-46
    • Koj, A.1    Frendo, J.2    Wojtczak, L.3
  • 10
    • 49749158181 scopus 로고
    • Isolation and properties of a β-mercaptopyruvate-cleaving copper enzyme
    • Kun E, Fanshier DW (1959) Isolation and properties of a β-mercaptopyruvate-cleaving copper enzyme. Biochim Biophys Acta 32:338-348
    • (1959) Biochim Biophys Acta , vol.32 , pp. 338-348
    • Kun, E.1    Fanshier, D.W.2
  • 11
    • 0020692658 scopus 로고
    • Developmental pattern, tissue distribution, and subcellular distribution of cysteine: α-ketoglutarate aminotransferase and 3-mercaptopyruvate sulfur-transferase activities in the rat
    • Kuo SM, Lea TC, Stipanuk MH (1983) Developmental pattern, tissue distribution, and subcellular distribution of cysteine: α-ketoglutarate aminotransferase and 3-mercaptopyruvate sulfur-transferase activities in the rat. Biol Neonate 43:23-32
    • (1983) Biol Neonate , vol.43 , pp. 23-32
    • Kuo, S.M.1    Lea, T.C.2    Stipanuk, M.H.3
  • 13
    • 0001113801 scopus 로고
    • Conversion of the α-keto analog of cysteine to pyruvate and sulfur
    • Meister A (1953) Conversion of the α-keto analog of cysteine to pyruvate and sulfur. Fed Proc 12:245
    • (1953) Fed Proc , vol.12 , pp. 245
    • Meister, A.1
  • 14
    • 0029003927 scopus 로고
    • Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily related to mitochondrial rhodanese. Striking similarity in active site amino acid sequence and the increase in the mercaptopyruvate sulfurtransferase activity of rhodanese by site-directed mutagenesis
    • Nagahara N, Okazaki T, Nishino, T (1995) Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily related to mitochondrial rhodanese. Striking similarity in active site amino acid sequence and the increase in the mercaptopyruvate sulfurtransferase activity of rhodanese by site-directed mutagenesis. J Biol Chem 270:16230-16235
    • (1995) J Biol Chem , vol.270 , pp. 16230-16235
    • Nagahara, N.1    Okazaki, T.2    Nishino, T.3
  • 15
    • 0029861910 scopus 로고    scopus 로고
    • Role of amino acid residues in the active site of rat liver mercaptopyruvate sulfurtransferase. cDNA cloning, overexpression, and site-directed mutagenesis
    • Nagahara N, Nishino T (1996) Role of amino acid residues in the active site of rat liver mercaptopyruvate sulfurtransferase. cDNA cloning, overexpression, and site-directed mutagenesis. J Biol Chem 271:27395-27401
    • (1996) J Biol Chem , vol.271 , pp. 27395-27401
    • Nagahara, N.1    Nishino, T.2
  • 16
    • 0022520391 scopus 로고
    • Reversible interconversion between sulfo- and desulfoxanthine dehydrogenase
    • Nishino T (1985) Reversible interconversion between sulfo-and desulfoxanthine dehydrogenase. Adv Exp Med Biol 195B: 259-262
    • (1985) Adv Exp Med Biol , vol.195 B , pp. 259-262
    • Nishino, T.1
  • 17
    • 0028557060 scopus 로고
    • Tissue and subcellular distribution of bound and acid-labile sulfur, and the enzymic capacity for sulfide production in the rat
    • Ogasawara Y, Isoda S, Tanabe S (1994) Tissue and subcellular distribution of bound and acid-labile sulfur, and the enzymic capacity for sulfide production in the rat. Biol Pharm Bull 17: 1535-1542
    • (1994) Biol Pharm Bull , vol.17 , pp. 1535-1542
    • Ogasawara, Y.1    Isoda, S.2    Tanabe, S.3
  • 18
    • 0021398312 scopus 로고
    • A purified precursor polypeptide requires a cytosolic protein fraction for import into mitochondria
    • Ohta S, Schatz G (1984) A purified precursor polypeptide requires a cytosolic protein fraction for import into mitochondria. EMBO J 3:651-657
    • (1984) EMBO J , vol.3 , pp. 651-657
    • Ohta, S.1    Schatz, G.2
  • 19
    • 0015896015 scopus 로고
    • The microcirculatory hepatic unit
    • Rappaport AM (1973) The microcirculatory hepatic unit. Microvas Res 6:212-228
    • (1973) Microvas Res , vol.6 , pp. 212-228
    • Rappaport, A.M.1
  • 20
    • 0000635069 scopus 로고
    • Crystalline rhodanese. Purification and physicochemical examination
    • Sörbo BH (1953) Crystalline rhodanese. Purification and physicochemical examination. Acta Chem Scand 7:1129-1136
    • (1953) Acta Chem Scand , vol.7 , pp. 1129-1136
    • Sörbo, B.H.1
  • 21
    • 0001211810 scopus 로고
    • Enzymic transfer of sulfur from mercaptopyruvate to sulfite or sulfinates
    • Sörbo BH (1957a) Enzymic transfer of sulfur from mercaptopyruvate to sulfite or sulfinates. Biochim Biophys Acta 24:324-329
    • (1957) Biochim Biophys Acta , vol.24 , pp. 324-329
    • Sörbo, B.H.1
  • 22
    • 0001354474 scopus 로고
    • Sulfite and complex-bound cyanide as sulfur acceptors for rhodanese
    • Sörbo BH (1957b) Sulfite and complex-bound cyanide as sulfur acceptors for rhodanese. Acta Chem Scand 11:628-633
    • (1957) Acta Chem Scand , vol.11 , pp. 628-633
    • Sörbo, B.H.1
  • 23
    • 0025337402 scopus 로고
    • Catabolism of cyst(e)ine by rat renal cortical tubules
    • Stipanuk MH, Rosa J, Hirschberger LL (1990) Catabolism of cyst(e)ine by rat renal cortical tubules. J Nutr 120:450-158
    • (1990) J Nutr , vol.120 , pp. 450-1158
    • Stipanuk, M.H.1    Rosa, J.2    Hirschberger, L.L.3
  • 24
    • 0016215747 scopus 로고
    • Role of 3-mercaptopyruvate sulfur-transferase in the formation of the iron-sulfur chromophore of adrenal ferredoxin
    • Taniguchi T, Kimura T (1974) Role of 3-mercaptopyruvate sulfur-transferase in the formation of the iron-sulfur chromophore of adrenal ferredoxin. Biochim Biophys Acta 364:284-295
    • (1974) Biochim Biophys Acta , vol.364 , pp. 284-295
    • Taniguchi, T.1    Kimura, T.2
  • 25
    • 0024817618 scopus 로고
    • Sulphur in biological systems: A possible regulatory role
    • Toohey JL (1989) Sulphur in biological systems: a possible regulatory role. Biochem J 264:625-632
    • (1989) Biochem J , vol.264 , pp. 625-632
    • Toohey, J.L.1
  • 26
    • 14444278105 scopus 로고
    • Physiologic significance and regulation of hepatocellular heterogeneity
    • Traber PG, Chianale J, Gumucio JJ (1988) Physiologic significance and regulation of hepatocellular heterogeneity. Gastroenterology 91:1263-1270
    • (1988) Gastroenterology , vol.91 , pp. 1263-1270
    • Traber, P.G.1    Chianale, J.2    Gumucio, J.J.3
  • 27
    • 0021777879 scopus 로고
    • 3-Mercaptopyruvate sulfurtransferase activity in guinea pig and rat tissues
    • Ubuka T, Hosaki Y, Nishina H, Ikeda T (1985) 3-Mercaptopyruvate sulfurtransferase activity in guinea pig and rat tissues. Physiol Chem Phys Med NMR 17:41-43
    • (1985) Physiol Chem Phys Med NMR , vol.17 , pp. 41-43
    • Ubuka, T.1    Hosaki, Y.2    Nishina, H.3    Ikeda, T.4
  • 28
    • 0015516536 scopus 로고
    • Purification and properties of mercaptopyruvate sulfurtransferase of Escherichia coli
    • Vachek H, Wood JL (1972) Purification and properties of mercaptopyruvate sulfurtransferase of Escherichia coli. Biochim Biophys Acta 258:133-146
    • (1972) Biochim Biophys Acta , vol.258 , pp. 133-146
    • Vachek, H.1    Wood, J.L.2
  • 29
    • 0023888996 scopus 로고
    • Relationship between structure and function in renal proximal tubule
    • Welling LW, Welling DJ (1988) Relationship between structure and function in renal proximal tubule. J Electron Microsc Tech 9:171-185
    • (1988) J Electron Microsc Tech , vol.9 , pp. 171-185
    • Welling, L.W.1    Welling, D.J.2
  • 30
    • 0000288062 scopus 로고
    • Mercaptopyruvate, a substrate for rhodanese
    • Wood J L, Fiedler H (1953) β-Mercaptopyruvate, a substrate for rhodanese. J Biol Chem 205:231-234
    • (1953) J Biol Chem , vol.205 , pp. 231-234
    • Wood, J.L.1    Fiedler, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.