蛋白质中的精氨酰残基与热稳定性
Arginyl residues and thermal stability in proteins.
作者信息
Qaw F S, Brewer J M
出版信息
Mol Cell Biochem. 1986 Aug;71(2):121-7. doi: 10.1007/BF00214770.
PMID:3534544
Abstract
Guanidination and amidination of bovine serum albumin, yeast enolase and yeast alcohol dehydrogenase were accompanied by increases in thermal stability at lower extents of modification. Decreases in thermal stability result from greater modification. These results support suggestions that surface guanidino groups (arginyl groups) are an important factor in thermal stability of proteins.
摘要
牛血清白蛋白、酵母烯醇化酶和酵母乙醇脱氢酶的胍基化和脒基化在较低修饰程度时伴随着热稳定性的增加。更高程度的修饰则导致热稳定性降低。这些结果支持了表面胍基（精氨酰基）是蛋白质热稳定性的一个重要因素的观点。
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