A biochemical study of the origin of arginine aminopeptidases in human gingival fluid

Abstract

The sources of enzymes hydrolysing N- l-arginyl-2-naphthylamine in human gingival fluid was elucidated mainly by determining the fractionation qualities of the enzymes on Sephadex G-100 Superfine columns. The material investigated included gingival fluid representing clinically different states, as well as centrifuged whole saliva, plaque water extract, serum and erythrocytes. All the clinically different states (G0, G1, and G2) displayed a similar fractionation pattern; four enzyme peaks (I, II, III and IV, in decreasing molecular weight order) were revealed in each gingival fluid material. The severity of inflammation increased the relative proportion of the enzymes. Clinically healthy gingiva produced fluid containing the same enzymes as fluid derived from diseased tissue. An enzyme resembling aminopeptidase B was present in all gingival fluids. It is suggested that the sources of the enzymes were as follows: I, serum or plaque (and possibly cellular elements of blood other than erythrocytes); II, serum (or cellular elements of blood other than erythrocytes); III, erythrocytes; IV, erythrocytes. Evidence for enzymes derived from plaque or whole mouth saliva was less convincing.