Smith B D, Byers P H, Martin G R
Proc Natl Acad Sci U S A. 1972 Nov;69(11):3260-2. doi: 10.1073/pnas.69.11.3260.
Three hydroxyproline-containing proteins secreted into the medium by human fibroblasts in culture were isolated and characterized. A minor fraction was identical to the collagen monomer. The major fraction was a form of procollagen, which contained, in addition to pro alpha and alpha chains, a component estimated to have a molecular weight of 250,000. This component was a dimer of pro alpha chains joined by disulfide bonds. The third fraction, much lower in hydroxyproline and hydroxylysine content, was of still greater size. Pro alpha chains were released upon denaturation and reduction, indicating that this fraction may contain pro alpha chains linked by disulfide bonds to noncollagenous material.
对培养的人成纤维细胞分泌到培养基中的三种含羟脯氨酸的蛋白质进行了分离和鉴定。一小部分与胶原蛋白单体相同。主要部分是一种前胶原形式,除了原α链和α链外,还含有一种估计分子量为250,000的成分。该成分是由二硫键连接的原α链二聚体。第三部分的羟脯氨酸和羟赖氨酸含量低得多,分子量更大。变性和还原后会释放出原α链,表明该部分可能包含通过二硫键与非胶原物质相连的原α链。