Inhibition, Restoration and Enhancement of Proteolytic Action by Polylysine and Polyglutamic Acid

Abstract

POLYELECTROLYTES of high molecular weight have been shown to inhibit a variety of enzymes in what Spensley and Rogers¹ have called macroanionic and macrocationic inhibition. This phenomenon is probably due to an interaction of the polyelectrolytes with the enzyme or the enzyme-substrate complex. The inhibition of pepsin by the polypeptide polyelectrolyte poly-L-lysine has been reported by Katchalski, Berger and Neumann². Polylysine has been shown to combine reversibly with albumin to form insoluble complexes which dissolve in the presence of excess of either component³. We have also studied the inhibition of the proteolytic action of pepsin by the macrocation, poly-L-lysine, and the reversal of this inhibition by excess polylysine, and the inhibition of trypsin by the macroanion, polyglutamic acid, as well as the restoration and enhancement of trypsin action by excess polyglutamic acid.