Jander R, Rauterberg J, Glanville R W
Eur J Biochem. 1983 Jun 1;133(1):39-46. doi: 10.1111/j.1432-1033.1983.tb07427.x.
Short-chain collagen was isolated from bovine and from human placenta after limited pepsin digestion. By reductive cleavage of disulfide bonds under non-denaturing conditions, mainly non-collagenous domains were cleaved off yielding a uniform component composed of three polypeptide chains with molecular masses between 37 kDa and 48 kDa in a nearly equimolar ratio. The chains (SC1*, SC2* and SC3*) were isolated and characterized. By comparison of peptide patterns obtained after various cleavage procedures, they could be identified as more or less shortened forms of SC1, SC2 and SC3, the isolation of which from bovine short-chain collagen has been described [Jander et al. (1981) Eur. J. Biochem. 114, 17-25]. The peptide patterns; as well as N-terminal sequence determination, give evidence for the genetic individuality of the three chains; the data so far available suggest that together they form one triple-helical structure which represents the collagenous domain of the basic molecular unit of short-chain collagen.
短链胶原蛋白是在有限的胃蛋白酶消化后从牛和人胎盘中分离出来的。在非变性条件下通过二硫键的还原裂解，主要切割掉非胶原蛋白结构域，得到一种由三条多肽链组成的均匀成分，其分子量在37 kDa至48 kDa之间，比例近乎等摩尔。分离并表征了这些链（SC1*、SC2和SC3）。通过比较各种裂解程序后获得的肽谱，可将它们鉴定为SC1、SC2和SC3或多或少的缩短形式，此前已描述了从牛短链胶原蛋白中分离它们的方法[扬德等人（1981年）《欧洲生物化学杂志》114卷，第17 - 25页]。肽谱以及N端序列测定证明了这三条链的基因个体性；目前可得的数据表明，它们共同形成一个三螺旋结构，该结构代表短链胶原蛋白基本分子单元的胶原结构域。
