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体外弹性蛋白交联。关于赖氨酰氧化酶作用于原弹性蛋白形成锁链素的影响因素研究。

Elastin cross-linking in vitro. Studies on factors influencing the formation of desmosines by lysyl oxidase action on tropoelastin.

作者信息

Narayanan A S, Page R C, Kuzan F, Cooper C G

出版信息

Biochem J. 1978 Sep 1;173(3):857-62. doi: 10.1042/bj1730857.

Abstract

The formation of isodesmosine and desmosine in vitro by the action of lysyl oxidase on tropoelastin was studied. The synthesis of desmosines occurred in the absence of additional substances. The formation of desmosines was not affected by removal of molecular O2 from the reaction medium nor was it affected by the lack of proline hydroxylation in tropoelastin. However, there was virtually no desmosine formation at 15 degrees C, a temperature not conducive to coacervation, indicating that coacervation is an important prerequisite for cross-linking.

摘要

研究了赖氨酰氧化酶作用于原弹性蛋白在体外形成异锁链素和锁链素的过程。锁链素的合成在没有其他物质的情况下发生。从反应介质中去除分子氧或原弹性蛋白中缺乏脯氨酸羟基化均不影响锁链素的形成。然而,在15摄氏度时几乎没有锁链素形成,该温度不利于凝聚,这表明凝聚是交联的重要前提。

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