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. 1984 Jan 1;217(1):303–308. doi: 10.1042/bj2170303

Stoichiometry of reactions of alpha 2-macroglobulin with trypsin and chymotrypsin.

I Björk, L J Larsson, T Lindblom, E Raub
PMCID: PMC1153210  PMID: 6199019

Abstract

The stoichiometry of the individual steps, i.e. polypeptide chain cleavage, hydrolysis of the putative thioester bond and conformational change, of the reaction between alpha 2-macroglobulin and trypsin or chymotrypsin was analysed. The chain cleavage was monitored by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, the thioester hydrolysis by both a spectroscopic and a fluorimetric technique and the conformational change by tryptophan fluorescence. A stoichiometry of close to 2:1 was obtained for all reactions. This finding indicates that the alpha 2-macroglobulin half-molecule is an independent functional unit of the inhibitor, within which co-operativity between the two subunits may occur.

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Selected References

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