AbstractA cDNA clone, MT‐c, encoding metalloprotease was isolated from snake (Agkistrodon halys brevicadus) venom gland cDNA library. Deduced amino acid sequence indicated that MT‐c is composed of a signal sequence, amino‐terminal propeptide, a central metalloprotease domain, and a Lys‐Gly‐Asp (KGD) disintegrin domain. The partial cDNA encoding metalloprotease and disintegrin domain was subcloned and expressed in E. coll. The expressed MT‐c protein was purified and successfully refolded into functional form retaining the enzyme activity. Analyses of the purified recombinant protease activity revealed that the enzyme hydrolyzes extraceUular matrix proteins including type I gelatin, type 1V and type V collagen, while type I, II, III collagens and fibronectin were insensitive to the proteolytic digestion. The recombinant enzyme was also able to degrade fibrinogen by specifically cleaving Aα chain of the protein.