Schneir M, Miller E J
Biochim Biophys Acta. 1976 Sep 28;446(1):240-4. doi: 10.1016/0005-2795(76)90114-8.
The Type III collagen molecule, alpha]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.
III型胶原分子[α(III)]3由三条α1(III)链组成，每条链含有两个半胱氨酸残基。然而，通过未能与烷基化试剂碘代[14C]乙酸和4-乙烯基吡啶形成衍生物判断，在变性的三聚体γ-III型胶原成分中未检测到游离巯基。这种巯基反应性的缺乏似乎不是由III型胶原与非胶原肽之间的二硫键结合导致的。总体而言，结果表明III型胶原分子的所有六个巯基都参与链间二硫键结合。
