Open Access. Powered by Scholars. Published by Universities.®

Biochemistry, Biophysics, and Structural Biology Commons

Open Access. Powered by Scholars. Published by Universities.®

Articles 1 - 4 of 4

Full-Text Articles in Biochemistry, Biophysics, and Structural Biology

Protein S-Thiolation In Hepatocytes Stimulated By T-Butyl Hydroperoxide, Menadione, And Neutrophils, Yuh-Cherng Chai, S. Hendrich, James Thomas Mar 1994

Protein S-Thiolation In Hepatocytes Stimulated By T-Butyl Hydroperoxide, Menadione, And Neutrophils, Yuh-Cherng Chai, S. Hendrich, James Thomas

Yuh-Cherng Chai

In order to examine potentially important S-thiolated proteins, ^3^5S-labeled hepatocytes were exposed to oxidative stress. A similar group of S-thiolated proteins including carbonic anhydrase III was observed in cells treated with t-butyl hydroperoxide, menadione, or stimulated neutrophils. The radioactive thiols bound to hepatocyte proteins were identified by HPLC and more than 85% was glutathione. In menadione-treated hepatocytes, proteins were gradually S-thiolated over 30 min and 25% of the cellular glutathione pool became protein-bound. In t-butyl hydroperoxide-treated cells, S-thiolation was more transient and 11% of the glutathione was protein-bound. Neutrophil-treated hepatocytes had nearly the same amount of protein S-thiolation (8 ...


S-Thiolation Of Individual Human Neutrophil Proteins Including Actin By Stimulation Of The Respiratory Burst: Evidence Against A Role For Glutathione Disulfide, Yuh-Cherng Chai, S. Ashraf, R. Johnson, James Thomas Mar 1994

S-Thiolation Of Individual Human Neutrophil Proteins Including Actin By Stimulation Of The Respiratory Burst: Evidence Against A Role For Glutathione Disulfide, Yuh-Cherng Chai, S. Ashraf, R. Johnson, James Thomas

Yuh-Cherng Chai

Protein S-thiolation, a reversible modification of protein sulfhydryls resulting in formation of mixed-disulfides, was studied in human neutrophils stimulated with phorbol diester to produce superoxide anion. Rapid S-thiolation of several proteins was examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Glutathione was identified as the primary protein-bound thiol by HPLC chromatography, contributing considerably more than 85% of the total. Minor amounts of homocysteine and/or cysteine were also detected as protein-bound thiols. During the first 30 min after stimulation, 10% of the cellular glutathione became protein bound (2 nmol/mg of protein). There was no increase in glutathione disulfide suggesting that ...


Protein S-Thiolation And Dethiolation, James Thomas, Yuh-Cherng Chai, Che-Hun Jung Dec 1993

Protein S-Thiolation And Dethiolation, James Thomas, Yuh-Cherng Chai, Che-Hun Jung

Yuh-Cherng Chai

No abstract provided.


S-Thiolation And Irreversible Oxidation Of Sulfhydryls On Carbonic Anhydrase Iii During Oxidative Stress: A Method For Studying Protein Modification In Intact Cells And Tissues, C. Lii, Yuh-Cherng Chai, W. Zhao, James Thomas, S. Hendrich Dec 1993

S-Thiolation And Irreversible Oxidation Of Sulfhydryls On Carbonic Anhydrase Iii During Oxidative Stress: A Method For Studying Protein Modification In Intact Cells And Tissues, C. Lii, Yuh-Cherng Chai, W. Zhao, James Thomas, S. Hendrich

Yuh-Cherng Chai

No abstract provided.