High hydrostatic pressure and enzymic activity: inhibition of multimeric enzymes by dissociation.
High hydrostatic pressure and enzymic activity: inhibition of multimeric enzymes by dissociation.
复制标题
高静水压和酶活性:通过解离抑制多聚酶。
DOI:
10.1016/0003-9861(71)90290-6
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发表时间:
1971
影响因子:
3.9
通讯作者:
J. T. Penniston
中科院分区:
文献类型:
--
作者:
J. T. Penniston
When precautions were taken to saturate enzymes with their substrates and to prevent pressure denaturation, it was found that the activities of multimeric enzymes were inhibited and the activities of monomeric enzymes stimulated by application of high hydrostatic pressure. Multimeric enzymes which were inhibited were mitochondrial ATPase (measured by hydrolysis of ATP or by ATP-32Piexchange activity), erythrocyte membrane ATPase, sarcotubular vesicle ATPase, pyruvate carboxylase, argininosuccinase, alkaline phosphatase, and creatine kinase. Monomeric enzymes which were stimulated were peroxidase, myokinase, trypsin, amylase, lysozyme and chymotrypsin. Both theoretical considerations and the results of experimental studies by previous workers show that high hydrostatic pressure will dissociate protein multimers which are held together by noncovalent interactions. This dissociation must be considered as the major determinant of the effect of pressure on enzymic systems which depend upon such protein-protein interactions for their activity. Since the category of multimeric enzymes includes a large proportion of known enzymes, dissaggregating effects must be considered as a major factor in investigating the effects of pressure on all cellular systems. This conclusion is particularly relevant to the study of deep-sea organisms. Their enzyme systems either must be monomeric, or must have stronger noncovalent interactions between multimers, in order to operate at the high pressures under which these organisms live.