Proteolytic Enzymes in Ischæmic Necrosis of Rat Kidney

Abstract

FEW results^1–4 have been published on the quantitative changes of intracellular proteinases during the manifestation of ischæmic necrosis, although these enzymes are considered to be essentially involved in this process. According to de Duve et al.⁵ several hydrolases are segregated within certain subcellular particles, thus prevented from acting on cell constituents. Various influences, for example, anoxia, provoke a release of these enzymes from their structures. In rat kidney, cathepsins B and D are known to be bound to such particles (droplets); enzymatic activities responsible for splitting L-leucine-β-naphthylamide (aminopeptidases (APs)) and azo casein (‘neutral’proteinases), however, derive from the microsomal fraction^6,7. This communication presents results of changes in these enzymatic activities in the course of ischsemic necrosis.