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胶原蛋白交联的化学性质。用氰基硼氢化钠还原皮肤、肌腱和骨骼产物的表征。

The chemistry of the collagen cross-links. Characterization of the products of reduction of skin, tendon and bone with sodium cyanoborohydride.

作者信息

Robins S P, Bailey A J

出版信息

Biochem J. 1977 May 1;163(2):339-46. doi: 10.1042/bj1630339.

DOI:10.1042/bj1630339
PMID:17400
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1164702/
Abstract

Reduction of tissues with sodium cyanoborohydride at pH7.4 gave results identical with those obtained by KBH4 treatment. On reduction with sodium cyanoborohydride at pH 4.4, however, a previously undetected basic compound was formed and was identified by mass spectrometry and chemical degradation techniques as dihydrohydroxymerodesmosine. Histidino-hydroxymerodesmosine was not present, and further analysis confirmed that reduced aldol, a mojor product of reduction with KBH4 at the lower pH, was also absent. These results, together with an analysis of the time course of the reduction, support previous assertions that histidino-hydroxymerodesmosine is an artifact [robins *Bailey (1973) Biochem. J. 135, 657-665] and suggests that the non-reduced form of hydroxymerodesmosine probably does not constitute a major intermolecular bond in vivo.

摘要

在pH7.4条件下用氰基硼氢化钠还原组织,得到的结果与用KBH4处理得到的结果相同。然而,在pH 4.4条件下用氰基硼氢化钠还原时,会形成一种先前未检测到的碱性化合物,通过质谱和化学降解技术鉴定为二氢羟基异二联赖氨酸。不存在组氨酸-羟基异二联赖氨酸,进一步分析证实,在较低pH值下用KBH4还原的主要产物还原醛醇也不存在。这些结果,连同对还原时间进程的分析,支持了先前关于组氨酸-羟基异二联赖氨酸是一种假象的论断[罗宾斯*贝利(1973年)《生物化学杂志》135卷,657 - 665页],并表明羟基异二联赖氨酸的未还原形式在体内可能不构成主要的分子间键。

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本文引用的文献

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Studies on the reduction of elastin. II. Evidence for the presence of alpha-aminoadipic acid delta-semialdehyde and its aldol condensation product.弹性蛋白降解的研究。II. α-氨基己二酸δ-半醛及其羟醛缩合产物存在的证据。
Biochemistry. 1969 Jul;8(7):2837-45. doi: 10.1021/bi00835a022.
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Intermediate labile intermolecular crosslinks in collagen fibres.胶原纤维中的中等不稳定分子间交联。
Biochim Biophys Acta. 1968 Aug 13;160(3):447-53. doi: 10.1016/0005-2795(68)90216-x.
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Chemistry of the collagen cross-links. Isolation and characterization of two intermediate intermolecular cross-links in collagen.胶原蛋白交联的化学性质。胶原蛋白中两种中间分子间交联的分离与表征。
Biochem J. 1970 May;117(5):819-31. doi: 10.1042/bj1170819.
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The nature of crosslinking in collagens from mineralized tissues.矿化组织中胶原蛋白的交联性质。
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The chemistry of the collagen cross-links. The characterization of fraction C, a possible artifact produced during the reduction of collagen fibres with borohydride.胶原蛋白交联的化学性质。C组分的特性,C组分是在用硼氢化物还原胶原纤维过程中可能产生的一种假象产物。
Biochem J. 1973 Dec;135(4):657-65. doi: 10.1042/bj1350657.
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Isolation of the crosslink, hydroxymerodesmosine, from borohydride-reduced collagen.从硼氢化物还原的胶原蛋白中分离交联物羟基异锁链素。
Biochim Biophys Acta. 1973 May 17;310(1):130-6. doi: 10.1016/0005-2795(73)90016-0.
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The chemistry of the collagen cross-links. Age-related changes in the reducible components of intact bovine collagen fibres.胶原蛋白交联的化学性质。完整牛胶原纤维可还原成分的年龄相关变化。
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Structure of two histidine-containing crosslinks from collagen.来自胶原蛋白的两种含组氨酸交联的结构。
J Biol Chem. 1973 Jan 25;248(2):393-402.
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Cross-linking of collagen.胶原蛋白的交联
Science. 1973 May 11;180(4086):561-6. doi: 10.1126/science.180.4086.561.