Resumo

HURTADO, L.; LERMA, L.; RODRIGUEZ, E.  e  YARLEQUE, A. Isolation and some biochemical properties of a hyaluronate glucanohydrolase from the venom of Lachesis muta, peruvian snake. Rev. Soc. Quím. Perú [online]. 2007, vol.73, n.4, pp.226-234. ISSN 1810-634X.

A proteic factor capable to produce hydrolysis into hyaluronic acid was purified from the venom of Lachesis muta, peruvian snake. Using two chromatographic steps: Sephadex G100 followed by CM-Sephadex C-50 columns equilibrated with 0,05M ammonium acetate buffer pH 5,0, purified factor was eluted from the second column with 0 - 0,7 M NaCl linear gradient with 51,4 folds, 38,6 of yield and 0,8% recovering protein. Isolated enzyme showed 5.0 optimus pH and 65 kDa as molecular weight by PAGE SDS. It is an alkaline glycoprotein containing 15,59% hexoses, 1,93% hexosamines and 0,92% sialic acid. Besides, 12 mM TLCK reduced to 40,04% the initial enzymatic activity, suggesting that histidine is involved into active site.

Palavras-chave : enzyme; venom; hyaluronic acid; isolation.

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