COLLAGEN CROSSLINKING - ISOLATION OF HYDROXYALDOL-HISTIDINE, A NATURALLY-OCCURRING CROSSLINK
COLLAGEN CROSSLINKING - ISOLATION OF HYDROXYALDOL-HISTIDINE, A NATURALLY-OCCURRING CROSSLINK
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DOI：
10.1016/0006-291x(75)90887-6
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发表时间：
1975-01-01
影响因子：
3.1
通讯作者：
GALLOP, PM
中科院分区：
文献类型：
--
作者：
HOUSLEY, T;TANZER, ML;GALLOP, PM
从牛皮肤胶原蛋白中分离出一种新的三功能交联物羟基醛-组氨酸。该化合物不能被硼氢化钠还原；用PMR光谱和挥发性衍生物的低、高分辨质谱对其进行了表征。这种交联与先前在纯胶原衍生肽中检测到的未知氨基酸相同。我们假定它是由肽基丙氨酸、羟丙氨酸和组氨酸缩合而成的。这是在胶原蛋白中发现的第一个非硼氢化物可还原交联的例子。
A new trifunctional crosslink, termed hydroxyaldol-histidine, was isolated from cow skin collagen. This compound was not reducible by sodium borohydride; it was characterized by PMR spectroscopy and by low and high resolution mass spectroscopy of volatile derivatives. This crosslink is identical to an unknown amino acid previously detected in pure collagen-derived peptides. We postulate that it arises by condensation of peptidyl allysine, hydroxyallysine and histidine. This is the first example of a non-borohydride reducible crosslink found in collagen.