THERMAL TRANSITION OF A NON-HYDROXYLATED FORM OF COLLAGEN - EVIDENCE FOR A ROLE FOR HYDROXYPROLINE IN STABILIZING TRIPLE-HELIX OF COLLAGEN
THERMAL TRANSITION OF A NON-HYDROXYLATED FORM OF COLLAGEN - EVIDENCE FOR A ROLE FOR HYDROXYPROLINE IN STABILIZING TRIPLE-HELIX OF COLLAGEN
复制标题
DOI：
10.1016/0006-291x(73)90961-3
复制
发表时间：
1973-01-01
影响因子：
3.1
通讯作者：
PROCKOP, DJ
中科院分区：
文献类型：
--
作者：
BERG, RA;PROCKOP, DJ
从α，α‘-联吡啶孵育的胚胎肌腱细胞中用0.1N冰醋酸提取非羟化型胶原蛋白，并用可控蛋白水解法进行纯化。结果表明，修饰后的原胶原蛋白由与胶原蛋白α1和α2链大小相同的多肽组成，并具有类似于胶原蛋白的旋光性热转变。然而，Tm值为24°，比来自相同来源的羟化形式的胶原的Tm值低15°。结果表明，羟基脯氨酸提高了胶原的热稳定性。
Protocollagen, a non-hydroxylated form of collagen, was extracted with cold 0.1 N acetic acid from embryonic tendon cells incubated with α,α′-dipyridyl and the protein was purified by controlled proteolytic digestion. The resulting modified protocollagen was shown to consist of polypeptides the same size as α1 and α2 chains of collagen and had a thermal transition by optical rotation similar to collagen. The Tmhowever was 24°, a value which was 15° lower than the Tmof an hydroxylated form of collagen from the same source. The results suggest that hydroxylated proline increases the thermal stability of collagen.