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
中科院分区:
文献类型:
--
作者:
AHERN, TJ;KLIBANOV, AM
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.