Kinin inactivating enzyme from mushroom Tricholoma conglobatum. III. Stability in the rat body and kinin suppression in vivo.

Publisher Website
Google Scholar
Abstract
The suppression of kinin action in the body by Shimeji kininase was studied in rat. This enzyme was purified from a mushroom Tricholoma conglobatum (Shimeji, in Japanese) and had the highest kinin inactivating activity among the ever known kininases from plants. The enzyme was stable in rat plasma for a long time in vitro. The enzyme also maintained the activity in the plasma in vivo and the loss of activity from the rat vascular system was too small even 1 hr after the intravenous injection of it. This enzyme markedly suppressed the hypotensive effect of bradykinin and the capillary permeability increase induced by bradykinin. In contrast with this, the hypotension caused by acetylcholine and the capillary permeability increase by histamine and serotonin were not suppressed by this enzyme. From these observation, this enzyme was considered to be able to block the kinin action in the body for a certain period due to the rapid kinin destruction by it. The enzyme also had the potent anti-inflammatory activity on the rat paw edema induced by carrageenin.

This publication has 0 references indexed in Scilit: