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“β - 本酶”的热稳定性和pH稳定性

Thermal and pH stability of "beta-benzyme".

作者信息

D'Souza V T, Lu X L, Ginger R D, Bender M L

出版信息

Proc Natl Acad Sci U S A. 1987 Feb;84(3):673-4. doi: 10.1073/pnas.84.3.673.

Abstract

The thermal and pH stability of "beta-benzyme", an artificial chymotrypsin based on beta-cyclodextrin, has been studied and compared with the stability of real chymotrypsin. Artificial chymotrypsin is vastly superior to real chymotrypsin with regard to both temperature and pH stability. The reasons for this increased stability are discussed.

摘要

对基于β-环糊精的人工胰凝乳蛋白酶“β-本酶”的热稳定性和pH稳定性进行了研究,并与天然胰凝乳蛋白酶的稳定性进行了比较。在温度和pH稳定性方面,人工胰凝乳蛋白酶都大大优于天然胰凝乳蛋白酶。文中讨论了其稳定性提高的原因。

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本文引用的文献

1
Elimination of cannibalistic denaturation by enzyme immobilization or inhibition.
Proc Natl Acad Sci U S A. 1981 Jul;78(7):4118-9. doi: 10.1073/pnas.78.7.4118.
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Ageing of alpha-chymotrypsin: Cannibalistic and hydroxide ion reactions.
Proc Natl Acad Sci U S A. 1981 Jul;78(7):4116-7. doi: 10.1073/pnas.78.7.4116.
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Structure of alpha-chymotrypsin refined at 1.68 A resolution.
J Mol Biol. 1985 Aug 20;184(4):703-11. doi: 10.1016/0022-2836(85)90314-6.

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