Incorporation of cystine into the proteins of regenerating wound tissue |
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| Affiliation: | 1. Department of Chemistry and Molecular Biology, Wallenberg Center for Molecular and Translational Medicine, University of Gothenburg, Göteborg, Sweden;2. Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Odense, Denmark;1. Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, SC, United States;2. Department of Drug Discovery and Biomedical Sciences, Medical University of South Carolina, Charleston, SC, United States;1. Department of Cell and Molecular Pharmacology & Experimental Therapeutics, College of Medicine, Medical University of South Carolina, Charleston, SC, United States;2. Hollings Cancer Center, Medical University of South Carolina, Charleston, SC, United States |
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| Abstract: | A procedure to distinguish between cystine bound into protein by peptide bonds and that associated with the protein as prosthetic groups by disulfide bonds only has been devised. This distinction is achieved by reaction of the cysteine and cystine in the protein with sodium sulfite in alkaline medium and simultaneous separation of the resulting thiosulfate derivatives by dialysis. Of the total cystine in regenerating wound tissue proteins, 6.6% is bound by disulfide bonds only. This fraction of the half-cystine residues turns over very much more rapidly than do the cystine residues in the protein bound by peptide bonds. The formation and turnover of liver proteins, as indicated by cystine-S35 incorporation, is much more rapid in wounded than in normal rats. Wounding also appears to have the effect of increasing the proportion of half-cystine residues linked to the liver proteins by disulfide bonds only. |
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