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Dissociation of proteinase-inhibitor complexes by trichloroacetate

✍ Scribed by Gary L. Gustafson; Donald J. Finn; Kamiar Moin

Book ID: 102630221
Publisher: Elsevier Science
Year: 1988
Tongue: English
Weight: 262 KB
Volume: 169
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(88)90271-0

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✦ Synopsis

It was demonstrated that the addition of high concentrations of the chaotrope, sodium trichloroacetate, to proteinase assays provided for a dissociation of proteinase-inhibitor complexes. The complexes evaluated contained a heat-stable, polypeptide inhibitor of cysteine proteinases isolated from the cellular slime mold, Dictyostelium discoideum. The proteinases that were present in separate complexes included either D. discoideum proteinases or the plant proteinase papain. The general assay procedures described may be useful in detection of endogenous proteinase-inhibitor complexes in many systems.

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