PMID: 2489059Feb 1, 1989Paper

Solid surface-catalysed inactivation of bovine alpha-chymotrypsin in dilute solution

International Journal of Biological Macromolecules
G Oshima

Abstract

Although loss of chymotrypsin activity in dilute solution deviated from first order kinetics at low enzyme concentration, it displayed first order kinetics at concentrations more than 4 nM. First order rate constants varied with the ratio of surface area to volume, with the kind of vessel containing the enzyme, and with the particular test material (DS, polybrene, lecithin or BSA) coating the vessel. The reaction was saturable at lower chymotrypsin concentrations in glass than in polypropylene tubes, while less enzyme was lost at high concentrations. All these facts showed that loss of enzyme activity is incompletely, but markedly, due to a solid surface-catalysed reaction. Intrinsic fluorescence of native chymotrypsin at pH values 8 and 3, and of active site-blocked enzyme, decreased with time at 37 degrees C. No extensive autolysis of chymotrypsin was observed during the time-dependent loss of enzyme activity. Therefore, the apparent loss of chymotrypsin activity in dilute solution was mainly due to an irreversible conformational change of the molecules, as associated with the solid-surface-catalysed reaction.

Citations

Feb 16, 2002·European Journal of Biochemistry·Anja I PekkarinenMarja-Leena Niku-Paavola
Oct 25, 1995·Biochimica Et Biophysica Acta·M C MasteW Norde
Jun 13, 2002·Journal of Agricultural and Food Chemistry·Anja I Pekkarinen, Berne L Jones
May 15, 1990·Thrombosis Research·G Oshima

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