JaLCDOI 10.18926/AMO/30897
FullText URL fulltext.pdf
Author Ikeda, Takahiro| Ubaka, Toshihiko| Ishino, Kazushi|
Abstract <p>The isoelectric point (pI) value of 3-mercaptopyruvate sulfurtransferase (MST) from human erythrocytes was determined to be 6.3 at 10 degrees C by isoelectric focusing in horizontal slab polyacrylamide gel containing 2% carrier ampholyte (pH 3-10). The value was determined by comparison with the electrofocused bands of bovine pancreatic ribonuclease A-glutathione mixed disulfides (RNase-SG), which were composed of 8 species containing 1 (RNase-SG1) through 8 (RNase-SG8) moles of glutathione per mole of ribonuclease A with different pI values ranging from 5.3 (RNase-SG8) to 8.8 (RNase-SG1). The pI value of the same enzyme in a 110,000 X g supernatant of rat liver was 5.9, which was the same as that of rat erythrocyte enzyme. Treatments of rat hemolysate with oxidized glutathione or diamide resulted in a shift of the pI of MST to a lower value, 5.7-5.5. This shift was inhibited when these treatments were performed in the presence of dithiothreitol. These results indicate that the treatment of the enzyme with oxidized glutathione results in the formation of enzyme-glutathione mixed disulfide.</p>
Keywords 3-mercaptopyruvate sulfurtransferase isoelectric point glutathione mixed disulfide isoelectric focusing
Amo Type Article
Published Date 1989-02
Publication Title Acta Medica Okayama
Volume volume43
Issue issue1
Publisher Okayama University Medical School
Start Page 1
End Page 7
ISSN 0386-300X
NCID AA00508441
Content Type Journal Article
language 英語
File Version publisher
Refereed True
PubMed ID 2718769
Web of Sience KeyUT A1989T938500001