CDNA cloning, expression and fibrin(ogen)olytic activity of two low-molecular weight snake venom metalloproteinases.

ABSTRACT: Two cDNA clones, AplVMP1 and AplVMP2, were isolated from a snake (Agkistrodon piscivorus leucostoma) venom gland cDNA library. The full-length cDNA sequence of AplVMP1 with a calculated molecular mass of 46.61 kDa is 1233 bp in length. AplVMP1 encodes PI class metalloproteinase with an open reading frame of 411 amino acid residues that includes signal peptide, pro-domain and metalloproteinase domains. The full-length cDNA of the AplVMP2 (1371 bp) has a calculated molecular mass of 51.16 kDa and encodes PII class metalloproteinase. The open reading frame of AplVMP2 with a 457 amino acid residues is composed of signal peptide, pro-domain, metalloproteinase and disintegrin domains. AplVMP1 and AplVMP2 showed 85% and 93% amino acid identical to PI class enzyme Agkistrodon contortrix laticinctu

SUBMITTER: Jia Y 

PROVIDER: S-EPMC3437927 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature