Mayne R, Vail M S, Miller E J
Proc Natl Acad Sci U S A. 1975 Nov;72(11):4511-5. doi: 10.1073/pnas.72.11.4511.
Chick embryo chondrocytes, in primary culture, initially synthesize only Type ii collagen (chain composition, [alpha1(II)13), as judged by two criteria: (i) carbosymethyl-cellulose chromatography of the denatured collagen, and (ii) carbosymethyl-cellulose chromatography of the cyanogen bromide peptides derived from the isolated chains. After a period of growth in 5-bromo-2'-deoxyuridine, however, synthesis of two different types of collagen could be detected after differential salt precipitation of the newly synthesized native collagens from neutral salt solutions at 2.2 M NaCl and subsequently at 0.01 M Na2hPO4. By criteria indicated above, the collagen precipitating at 2.2 M NaCl was identified as Type I collagen (chain composition, [alpha(I)]2alpha2), whereas the collagen subsequently precipitated at 0.01 M Na2HPO4 was found to be comprised entirely of alpha1(I) chains, indicating a chain composition, alpha]3. We propose to designate the latter type of molecule as the Type I trimer.
原代培养的鸡胚软骨细胞最初仅合成Ⅱ型胶原蛋白(链组成,[α1(II)]3),这是根据两个标准判断的:(i)变性胶原蛋白的羧甲基纤维素色谱分析,以及(ii)从分离链衍生的溴化氰肽的羧甲基纤维素色谱分析。然而,在5-溴-2'-脱氧尿苷中生长一段时间后,在将新合成的天然胶原蛋白从2.2 M NaCl的中性盐溶液中,随后从0.01 M Na2HPO4中进行分级盐沉淀后,可以检测到两种不同类型胶原蛋白的合成。根据上述标准,在2.2 M NaCl下沉淀的胶原蛋白被鉴定为Ⅰ型胶原蛋白(链组成,[α(I)]2α2),而随后在0.01 M Na2HPO4下沉淀的胶原蛋白被发现完全由α1(I)链组成,表明链组成为[α(I)]3。我们建议将后一种类型的分子指定为Ⅰ型三聚体。