Resumen

CISNEROS, Yori; LAZO, Fanny; GUTIERREZ, Susana  y  YARLEQUE, Armando. Características bioquímicas de una proteína antibacteriana aislada del veneno de Lachesis muta "Shushupe". Rev. Soc. Quím. Perú [online]. 2006, vol.72, n.4, pp.187-196. ISSN 1810-634X.

An L-amino acid oxidase from the venom of Lachesis muta snake was obtained through CM-Sephadex C-50 cation-exchange chromatography followed by Sephadex G-100 SF gel filtration at pH 6 with 0,1M ammonium acetate buffer. LAO was recovered with 32% of yield and 8 folds showing a single electrophoretical band on PAGE-SDS with 60,6 kDa molecular weight under reduction conditions. It is an acid protein and homodimeric protein with 7,5 as optimum pH using L-leucine as substrate. Dialysis produced a severe effect on this activity, while 7,5 mM Zn²⁺ ions produced low activity until 63%. In the same manner, the enzyme was inhibited by L-cysteine, iodoacetate and glutation. Glutamic acid and EDTA were unaffected agents. Assays on Staphylococcus aureus and Vibrio cholerae bacterial cultures showed a potent grow inhibition. Therefore LAO is an antibacterial protein either on Gram positive and Gram negative bacterials.

Palabras clave : Venom; snake; L-amino acid oxidase; enzyme; antibacterial.