THE MECHANISM OF IRREVERSIBLE ENZYME INACTIVATION AT 100-DEGREES-C

THE MECHANISM OF IRREVERSIBLE ENZYME INACTIVATION AT 100-DEGREES-C
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DOI:
10.1126/science.4001942
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发表时间:
1985-01-01
期刊:
影响因子:
56.9
通讯作者:
KLIBANOV, AM
KLIBANOV, AM
中科院分区:
综合性期刊1区
文献类型:
--
作者:
AHERN, TJ;KLIBANOV, AM

文献摘要

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在与酶催化相关的pH范围内,定量地阐明了酶不可逆热失活的机理。导致蛋清溶菌酶在100℃不可逆失活的过程是天冬酰胺残基的脱酰胺、天冬氨酸残基上的多肽键的水解、二硫键的破坏和不正确的(杂乱)结构的形成;它们的相对贡献取决于pH。
The mechanism of irreversible thermoinactivation of an enzyme has been quantitatively elucidated in the pH range relevant to enzymatic catalysis. The processes causing irreversible inactivation of hen egg-white lysozyme at 100°C are deamidation of asparagine residues, hydrolysis of peptide bonds at aspartic acid residues, destruction of disulfide bonds, and formation of incorrect (scrambled) structures; their relative contributions depend on thepH.