Snake venom hemorrhagins.

Viperine and crotaline snake venoms contain one or more hemorrhagic principles called hemorrhagins. These are zinc-containing metalloproteases characterized by the presence of a protease domain, with additional domains in some of them. They act essentially by degrading the component proteins of basement membrane underlying capillary endothelial cells.

Characterization of a membrane protease from rat submaxillary-gland mitochondria that possess thrombin-like activity.

A membrane protease possessing thrombin-like activity was purified to homogeneity from mitochondria of rat submaxillary gland. The molecular mass of the enzyme was determined to be 45 kDa by SDS/PAGE under reducing conditions and by gel filtration on a Sephadex G-100 column. The enzyme is a glycoprotein and has an isoelectric point of 3.

A new blood-coagulating protease in mitochondrial membranes of rat submaxillary glands. Purification and characterization of protease and its blood-coagulating activity.

An integral membrane protease was solubilized and purified to homogeneity from rat submaxillary mitochondria. The purified enzyme could coagulate rabbit plasma. The molecular mass of the enzyme is 22 kDa on SDS-polyacrylamide gel electrophoresis under reducing conditions and 24 kDa on gel filtration on a Sephadex G-100 column.

Neutralization of pathophysiological manifestations of Russell's viper envenoming by antivenom raised against gamma-irradiated toxoid.

Rabbits were immunized against gamma-irradiated (100 krads) Russell's viper venom toxoid adsorbed to aluminium phosphate gel. The antivenom (0.1 ml) neutralized 5 LD50, 8 minimum hemorrhagic doses (MHD) and 14 minimum necrotic doses (MND) of venom.