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软骨蛋白聚糖的碱性裂解和硼氢化钠还原反应

The alkaline cleavage and borohydride reduction of cartilage proteoglycan.

作者信息

Robinson H C, Hopwood J J

出版信息

Biochem J. 1973 Jul;133(3):457-70. doi: 10.1042/bj1330457.

Abstract

A method for the rapid isolation and purification of proteoglycan by using neutral solutions of LiBr for extraction and density-gradient centrifugation is described. The effect of 0.5m-KOH on isolated proteoglycan has been studied by using NaB(3)H(4) to reduce and label the chondroitin sulphate chains released. This study has established: (a) that at least 95% of the chondroitin sulphate chains are attached to the proteoglycan by alkali-labile bonds between xylose and serine; (b) that random degradation of the chondroitin sulphate chains does not occur to any significant extent; (c) that the method is convenient for the determination of polysaccharide number-average molecular weights.

摘要

本文描述了一种通过使用溴化锂中性溶液进行提取和密度梯度离心来快速分离和纯化蛋白聚糖的方法。通过使用硼氢化钠(NaB(3)H(4))还原并标记释放出的硫酸软骨素链,研究了0.5m - KOH对分离出的蛋白聚糖的影响。该研究确定了:(a)至少95%的硫酸软骨素链通过木糖和丝氨酸之间的碱不稳定键连接到蛋白聚糖上;(b)硫酸软骨素链不会发生显著程度的随机降解;(c)该方法便于测定多糖的数均分子量。

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