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. 1982 Sep 1;205(3):529–534. doi: 10.1042/bj2050529

Studies on the temperature-dependent autoinhibition of human plasma kallikrein I.

P R Levison, G Tomalin
PMCID: PMC1158517  PMID: 6924583

Abstract

At 37 degrees C, human plasma kallikrein I follows Michaelis-Menten behaviour and exhibits a normal linear relationship between the initial velocity of hydrolysis of Ac-Pro-Phe-Arg-OMe,HCl and enzyme concentration in the range 0--150 pM. At temperatures of 30 degrees C and below substantial deviations from linearity are observed over the same enzyme concentration range. The temperature-dependent autoinhibition of kallikrein I activity is reversible and is not due to low-molecular-weight endogenous inhibitors or cofactors. The kinetic effect is apparently due to aggregation and can be abolished by the addition of sodium deoxycholate.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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