[Long-term and acute toxicity of kallikrein from the venom of Agkistrodon hlays Pallas].
A novel serine protease with high purity was extracted from the venom of Agkistrodon hlays Pallas using monoclonal antibody affinity chromatography. This protease releases bradykinin and has arginine esterase activity without being activated. After purification, its hydrolytic activity exceeded 800 U/mg, far higher than its counterparts from mammalian sources. The purity of the kininogenase could exceed 95%. The acute toxicity and the long-term toxicity of this kallikrein was studied for its potential clinical application. The maximum tolerance dose in adult was 150,000 times greater than the maximum applied dose, and long-term administration at the dose 50 times of allowed clinical dose did not obviously after the animals' body weight, survival condition, liver function, renal function, or blood routines, suggesting the extremely low toxicity of the kallidrein.
Zhang
Ying
Y
Graduate School of the Chinese Academy of Sciences, Beijing 100009, China. zhying190@sina.com
Ma
Biao
B
Lin
Yong-qi
YQ
Luo
Yun-bo
YB
D017836:Agkistrodon; D000818:Animals; D001920:Bradykinin / Q000378:metabolism; D003435:Crotalid Venoms / Q000633:toxicity*; D007610:Kallikreins / Q000633:toxicity*; D020714:Maximum Tolerated Dose; D051379:Mice; D008807:Mice, Inbred BALB C; D012697:Serine Endopeptidases / Q000633:toxicity; D023382:Toxicity Tests, Acute
D003435:Crotalid Venoms; D007610:Kallikreins; D012697:Serine Endopeptidases; D001920:Bradykinin