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J.Health Sci., 48(5), 399-403, 2002
Physical Exercise Induces Oxidation of Plasma Protein Thiols to Cysteine Mixed Disulfides in Humans
Takayo Inayama,*, a, b Misato Kashiba,a Jun Oka,a Mitsuru Higuchi,a Keizo Umegaki,a Makoto Saito,c Yorihiro Yamamoto,d and Mitsuo Matsudae
aNational Institute of Health and Nutrition, 1-23-1 Toyama, Shinjuku-ku, Tokyo 162-8636, Japan, bSendai Shirayuri Women's College, 6-1 Honda-cho, Izumi-ku, Sendai city, Miyagi 981-3107, Japan, cOtsuma Women's University, 12 Sanban-cho, Chiyoda-ku, Tokyo 102-8357, Japan, dUniversity of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan, and eUniversity of Tsukuba, 1-1-1 Tennodai, Tsukuba city, Ibaraki 305-0006, Japan
We have reported that strenuous physical exercise causes a decrease in protein-bound sulfhydryl groups (p-SHs), such as albumin cysteine residues, in human plasma (Inayama et al., 1996, Life Sci., 59, 573-578). We further investigated the fate of plasma protein thiols after moderate exercise. Six untrained healthy female volunteers ran for 30-min at the individual ventilatory threshold. We observed an increase in protein cysteine mixed disulfides (p-S-Cys) after running, as evidenced by reducing plasma proteins with dithiothreitol to detect the increase of cysteine, along with the concomitant decrease in p-SHs in plasma. However, plasma protein-bound glutathione (GSH) and S-nitroso-protein were undetectable before and after exercise. Test tube experiments suggest that p-S-Cys are probably formed by the hydrolysis of protein GSH mixed disulfides by gamma-glutamyltranspeptidase and peptidase, and/or by the oxidative addition of p-SHs to cystine.
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