The influence of glycosylation on the thermal stability of ribonuclease

被引：11
|
作者：
Pfeil, W [1 ]
机构：
[1] Univ Potsdam, Inst Biochem & Biol, D-14476 Golm, Germany
来源：
THERMOCHIMICA ACTA | 2002年 / 382卷 / 1-2期
关键词：
ribonuclease; glycosylation; differential scanning microcalorimetry;
D O I：
10.1016/S0040-6031(01)00727-4
中图分类号：
O414.1 [热力学];
学科分类号：
摘要：
Using DSC, the thermal unfolding of RNase A, RNase B, and two partly deglycosylated RNase B forms was studied. The oligosaccharide side chain leads to slight protein stabilization. The conformational stability at pH 4.0 amounts to DeltaG(25degreesC) = 34.5, 34.6, 33.7, and 32.8 kJ mol(-1) for RNase B, Man(1)-RNase, GlnNAc(1)-RNase, and RNase A, respectively. The heat capacity remains the same for glycosylated and deglycosylated protein. These results are consistent with a proposed hydrogen bond of Lys37 with GlnNAc-1. (C) 2002 Elsevier Science B.V. All rights reserved.
引用
收藏
页码：169 / 174
页数：6
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