Dissociation of proteinase-inhibitor complexes by trichloroacetate.
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.
Gustafson
G L
GL
Department of Microbiology, University of Montana, Missoula 59812.
Finn
D J
DJ
Moin
K
K
D015853:Cysteine Proteinase Inhibitors; D004023:Dictyostelium / Q000201:enzymology; D010450:Endopeptidases; D010206:Papain; D011480:Protease Inhibitors; D011485:Protein Binding; D014238:Trichloroacetic Acid
D015853:Cysteine Proteinase Inhibitors; D011480:Protease Inhibitors; D014238:Trichloroacetic Acid; D010450:Endopeptidases; D010206:Papain