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Antitumoural Effect of an l ‐Amino Acid Oxidase Isolated from Bothrops jararaca Snake Venom
Author(s) -
De Vieira Santos Mariana M.,
Sant’Ana Carolina D.,
Giglio José R.,
Da Silva Reinaldo J.,
Sampaio Suely V.,
Soares Andreimar M.,
Fecchio Denise
Publication year - 2008
Publication title -
basic and clinical pharmacology and toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.805
H-Index - 90
eISSN - 1742-7843
pISSN - 1742-7835
DOI - 10.1111/j.1742-7843.2008.00229.x
Subject(s) - bothrops jararaca , venom , oxidative deamination , snake venom , sephadex , biochemistry , chemistry , gel electrophoresis , amino acid , polyacrylamide gel electrophoresis , size exclusion chromatography , sepharose , microbiology and biotechnology , enzyme , biology
An l ‐amino acid oxidase (BjarLAAO‐I) from Bothrops jararaca snake venom was highly purified using a stepwise sequential chromatography on Sephadex G‐75, Benzamidine Sepharose and Phenyl Sepharose. Purified BjarLAAO‐I showed a molecular weight around 60,000 under reducing conditions and about 125,000 in the native form, when analysed by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and gel filtration, respectively. BjarLAAO‐I is a homodimeric acidic glycoprotein, pI ~5.0, and N‐terminal sequence showing close structural homology with other snake venom LAAOs. The purified enzyme catalysed the oxidative deamination of l ‐amino acids, the most specific substrate being l ‐Phe. Five amino acids, l ‐Ser, l ‐Pro, l ‐Gly, l ‐Thr and l ‐Cys were not oxidized, clearly indicating a significant specificity. BjarLAAO‐I significantly inhibited Ehrlich ascites tumour growth and induced an influx of polymorphonuclear cells, as well as spontaneous liberation of H 2 O 2 from peritoneal macrophages. Later, BjarLAAO‐I induced mononuclear influx and peritoneal macrophage spreading. Animals treated with BjarLAAO‐I showed higher survival time.