Seasonal changes in the content of some sulfur compounds and sulfur-rich cytoplasmic granules in hepatocytes of the frog rana temporaria

Acta Biologica Cracoviensia Series Zoologia

Volumn 42, Issue , 2000, Pages 99-102

  Wröbel', Maria ^a   Sura, Piotr ^a   Srebro, Zbigniew ^a  

^a JAGIELLONIAN UNIVERSITY MEDICAL COLLEGE   (Poland)

Author keywords

Cysteine; Frog liver; Glutathione; Gomori positive granules; Sulfane sulfur; Sulfurtransferases

Indexed keywords

EID: 31344448652     PISSN: 0001530X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (22)

1. DUDEK, M., J. FRENDO, and A. Ko.i. 1980. Subcellular compartmentation of rhodanese and 3-mercaptopyruvate sulphurtransferase in the liver of some vertebrate species. Comp. Biochem. Physiol. 65B: 383-386.
2. FINAZZI-AGRO, A., c. CANNELLA, M. T. GRAZIANI, and D. A. CAVALUNI. 1971. A possible rôle for rhodanese: thé formation of "labile" sulfur from thiosulfate. FEES Lett. 16: 172-174.
3. GAITONDE, M. K. 1967. A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acid. Biochem. J. 104: 627-633.
4. KUN, E. 1957. The reaction of -mercaptopyruvate with lactic dehydrogenase of heart muscle. Biochim. Biophys. Ada 25: 135-137.
5. MATSUO, Y., and D. M. GREENBERG. 1958. A crystalline enzyme that cleaves homoserine and cystathionine. J. biol. Client. 230: 545-560
6. OGASAWARA, Y., S. ISODA, and S. TANABE. 1994. Tissue and subcellular distribution of bound and acid-labile sulfur, and the enzymic capacity for sulfide production in the rat. Biol. Pharrnacol. Bull. 17: 1535-1542.
7. OGASAWARA, Y, S. ISODA, and S. TANABE. 1995. Reconstitution of an iron-sulfur cluster with bound sulfur: a possible source of acid-labile sulfur in biological systems. Biol. Pharniacol. Bull. 18: 1045-1048.
8. OGASAWARA, Y, S. ISODA, K. ISHII, and S. TANABE. 1997. Modification of liver cytosol enzyme activities promoted in vitro by reduced species generated from cystine with cystathionase. Biochim. Biophys. Ada 1334: 33-43.
9. OGASAWARA, Y., S. ISODA, and S. TANABE. 1998. A labile sulfur in trisulfide affects cytochrome P-450 dependent lipid peroxidation in rat liver microsomes. Toxicol. Lett. 99: 191-198.
10. OGASAWARA, Y, S. ISODA, and S. TANABE. 1999. Antioxidant effect of albumin-bound sulfur in lipid peroxidation of rat liver microsomes. Biol. Pharmacol. Bull. 22: 441-445.
11. PEARSE A. G. E. 1960 Histochemistry, Theoretical and applied. London, Churchill.
12. SöRBO B. 1955 Rhodanese. In: S. R Colowick and N. O. Kaplan [eds.], Methods in Enzymology 2, 334-337. Academic Press, New York.
13. SREBRO Z., H. LACH, and P. SURA. 1996. Gomori-positive and sulphur-rich granules in hepatocytes of various species of frogs. Acta Biol. Cracov. Ser. ZooJ. 38: 1-3.
14. STIPANüK, M. H. I986. Metabolism of sulfur-containing amino acids. Annu. Rev. Nutr. 6:179-209.
15. TIETZE, F. 1969. Enzymatic method for quantitative determination of nanogram amounts of total and oxidized glutathione. Anal. Biochem. 27: 502-522.
16. TOOHEY, J. L. 1989. Sulphane sulphur in biological systems: a possible regulatory role. Biochem. J. 264: 625-632.
17. VALENTINE, W. N., and J. K. FRANKENFELD. 1974. 3-Mercaptopyruvate sulfurtransferase (EC 2.8.1.2): A simple assay adapted to human blood cells. Clin. Chim. Acta. 51: 205-210.
18. WESTLEY, J. 1980. Rhodanese and the sulfane pool. In: W. B. Jacoby [ed.], Enzymatic basis of detoxification. 245-262. Academic Press, New York.
19. WOOD, J. L. 1982. Biochemical functions of persulfides. Adv. Exp. Med. Biol. 148: 327-342.
20. WOOD, J. L. 1987. Sulfane sulfur. In: W. B. Jacoby, and O. W. Griffith (eds.], Methods in Enzymology 143, 25-29. Academic Press, San Diego.
21. WRöBEL M., P. SURA, and Z. SREBRO. 2000. Sulfurtransferases and the content of cysteine, glutathione and sulfane sulfur in tissues of the frog Rana temporaria. Camp. Biochem. Physiol. 125B: 211-217.
22. WRöBEL, M., T. UBUKA, W-B. YAO, and T. ABE. 1997. L-cysteine metabolism in guinea pig and rat tissues. Comp. Biochem. Physiol. 116B: 223-226.