Strawich E, Glimcher M J
J Biol Chem. 1983 Jan 10;258(1):555-62.
The hydroxylation of lysine in embryonic chick long bone and mandibular collagen was found to be approximately 3-fold greater than that of the collagens of adult animals. In contrast, no significant difference was found in extent of lysine hydroxylation of the collagens of frontal bones of embryos and postnatal animals. Both histochemical and biochemical evidence established that full thickness diaphyseal bone samples contained cartilage and, consequently, type II collagen which undoubtedly contributed to the higher hydroxylysine contents of young postnatal animals reported previously. DEAE ion exchange chromatography of the alpha 1(I) chains of lathyritic long bone and mandibular collagens isolated by carboxymethyl-cellulose ion exchange chromatography showed considerable heterogeneity, whereas the alpha 1(I) chains obtained from lathyritic frontal bone collagen did not. Three fractions of alpha 1(I) chains of long bones and mandibular collagen were isolated which differed significantly in their hydroxylysine contents. The relative proportion of the three peaks changed as a function of embryonic age and maturation: more of the alpha 1(I) chains with the highest hydroxylysine content was present in the collagen synthesized earliest during embryonic development. This is consistent with results which demonstrated that the collagens synthesized earliest during embryonic and postnatal development had the highest hydroxylysine contents.
研究发现，胚胎期鸡的长骨和下颌骨胶原蛋白中赖氨酸的羟基化程度比成年动物的胶原蛋白约高3倍。相比之下，胚胎和出生后动物额骨胶原蛋白的赖氨酸羟基化程度没有显著差异。组织化学和生物化学证据均表明，全层骨干骨样本中含有软骨，因此含有II型胶原蛋白，这无疑是先前报道的出生后幼小动物羟基赖氨酸含量较高的原因。对通过羧甲基纤维素离子交换色谱法分离得到的致跛行长骨和下颌骨胶原蛋白的α1(I)链进行DEAE离子交换色谱分析，结果显示出相当大的异质性，而从致跛行额骨胶原蛋白中获得的α1(I)链则没有。分离出了长骨和下颌骨胶原蛋白α1(I)链的三个组分，它们的羟基赖氨酸含量有显著差异。这三个峰的相对比例随胚胎年龄和成熟度而变化：在胚胎发育早期合成的胶原蛋白中，含有最高羟基赖氨酸含量的α1(I)链比例更高。这与以下结果一致，即胚胎期和出生后发育早期合成的胶原蛋白具有最高的羟基赖氨酸含量。
