Artigo Acesso aberto Revisado por pares

Amino acid sequence of a Crotalus atrox venom metalloproteinase which cleaves type IV collagen and gelatin

1989; Elsevier BV; Volume: 264; Issue: 20 Linguagem: Inglês

10.1016/s0021-9258(18)80102-8

ISSN

1083-351X

Autores

John D. Shannon, Eugenia N. Baramova, Jón B. Bjarnason, Jay W. Fox,

Tópico(s)

Healthcare and Venom Research

Resumo

The hemorrhagic toxin Ht-d from venom of the Western diamondback rattlesnake is a metalloproteinase with a molecular weight of 23,234. Peptides were obtained from enzymatic and chemical digestions, separated by reverse-phase chromatography, and sequenced in a gas-phase sequenator. The sequence showed a putative zinc binding site similar to that of thermolysin and other metalloproteinases but no overall significant similarity to the sequences of other metalloproteinases and may represent a new subfamily of metalloproteinases. Ht-d was shown to degrade type IV collagen and gelatin types I, III, and V but not interstitial collagens. The digestion of type IV collagen and other basement membrane proteins may allow this proteinase to disrupt capillary membranes causing hemorrhage in surrounding tissues.

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