Studies on the sulfhydryl groups in type III collagen.
The Type III collagen molecule, [alpha](III)]3, is comprised of three alphal(III) chains each of which contains two cysteinyl residues. Free sulfhydryl groups, however, could not be detected in the denatured, trimeric gamma-component of Type III collagen as judged by the failure to form derivatives with the alkylating reagents iodo-[14C]acetic acid and 4-vinylpyridine. This absence of sulfhydryl group reactivity did not appear to result from disulfide-binding between Type III collagen and noncollagenous peptides. Collectively, the results indicate that all of the six sulfhydryl groups of the Type III collagen molecule participate in interchain disulfide-bonding.
D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D003094:Collagen; D006801:Humans; D007223:Infant; D007461:Iodoacetates; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding; D011487:Protein Conformation; D012867:Skin; D013438:Sulfhydryl Compounds / Q000032:analysis
D000596:Amino Acids; D007461:Iodoacetates; D010446:Peptide Fragments; D013438:Sulfhydryl Compounds; D003094:Collagen