Purification and enzymatic characterization of a novel metalloprotease from Lachesis muta rhombeata snake venom.

ABSTRACT:

Background

Lachesis muta rhombeata (Lmr) is the largest venomous snake in Latin America and its venom contains mainly enzymatic components, such as serine and metalloproteases, L-amino acid oxidase and phospholipases A₂. Metalloproteases comprise a large group of zinc-dependent proteases that cleave basement membrane components such as fibronectin, laminin and collagen type IV. These enzymes are responsible for local and systemic changes, including haemorrhage, myonecrosis and inflammation. This study aimed the isolation and enzymatic characterization of the first metalloprotease (Lmr-MP) from Lmr venom (LmrV).

Methods and results

Lmr-MP was purified through two chromatographic steps and submitted to enzymatic characterization. It showed proteolytic activit

SUBMITTER: Cordeiro FA 

PROVIDER: S-EPMC6251203 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature