The separation and amino acid analysis of collagen crosslinks on an extended basic ion-exchange column.
The separation and amino acid analysis of collagen crosslinks on an extended basic ion-exchange column.
复制标题
在扩展碱性离子交换柱上胶原交联的分离和氨基酸分析。
DOI:
10.1016/0003-2697(81)90486-3
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发表时间:
1981
影响因子:
2.9
通讯作者:
Tanzer,ML
中科院分区:
文献类型:
--
作者:
Housley,TJ;Tanzer,ML
The major reducible crosslinks found in collagen were separated and analyzed on an extended basic amino acid analyzer column. Reaction with ninhydrin allows the direct analysis of collagen crosslinks, including hydroxyaldol-histidine, a naturally occurring, nonreducible crosslink. In addition to known crosslinks, direct amino acid analysis of tissue hydrolysates reveals the presence of an unknown, ninhydrin-reactive component, in both NaB3H4-reduced and unreduced collagenous tissues. Initial fractionation of hydrolysates on a Bio-Gel P-2 gel filtration column provides partial separaton of amino acids and crosslinks and enables more direct analysis of the crosslinks present in the samples, as well as detecting potential new crosslinks. The results also show that, prior to NaB3H4reduction, substantial amounts of known crosslinks are normally present in bovine skin and bone.