Control of enzymatic degradation of hyaluronan by divalent cations

被引：24

作者：

Vercruysse, KP ^{[1
]}

Ziebell, MR ^{[1
]}

Prestwich, GD ^{[1
]}

机构：

[1] Univ Utah, Dept Med Chem, Salt Lake City, UT 84112 USA

来源：

CARBOHYDRATE RESEARCH | 1999年 / 318卷 / 1-4期

关键词：

hyaluronidase; hyaluronan; gel-permeation chromatography; perfusion anion-exchange chromatography;

D O I：

10.1016/S0008-6215(99)00087-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Enzymatic degradation of hyaluronan (HA) by testicular hyaluronidase (HAase, hyaluronate 4-glucanohydrolase) requires inclusion of mono- or divalent cations in the reaction mixture. Most divalent cations activated HAase with equal potency; however, Cu(2+) suppressed degradation, and Ca(2+) showed a concentration-dependent regulation of size of the oligosaccharide products. Careful selection of HAase assay parameters is critical for discovery of novel HAase inhibitors and for preparation of controlled-size oligosaccharide fragments. (C) 1999 Elsevier Science Ltd. All rights reserved.

引用

页码：26 / 37

页数：12

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