%0 Journal Article
%T Purification of an L-amino acid oxidase from Bungarus caeruleus (Indian krait) venom
%A More
%A SS
%A Kiran
%A KM
%A Veena
%A SM
%A Gadag
%A JR
%J Journal of Venomous Animals and Toxins including Tropical Diseases
%D 2010
%I Centro de Estudos de Venenos e Animais Pe?onhentos - CEVAP, Universidade Estadual Paulista - UNESP
%R 10.1590/S1678-91992010005000002
%X snake venoms are rich in enzymes such as phospholipase a2, proteolytic enzymes, hyaluronidases and phosphodiesterases, which are well characterized. however, l-amino acid oxidase (lao ec.1.4.3.2) from snake venoms has not been extensively studied. a novel l-amino acid oxidase from bungarus caeruleus venom was purified to homogeneity using a combination of ion-exchange by deae-cellulose chromatography and gel filtration on sephadex£¿ g-100 column. the purified monomer of lao showed a molecular mass of 55 ¡À1 kda estimated by sds-page. the specific activity of purified lao was 6,230 ¡À 178 u/min/mg, versus 230 ¡À 3.0 u/min/mg for the whole desiccated venom, suggesting a 27-fold purification with a 25% yield. optimal ph and temperature for maximum purified enzyme activity were 6.5 and 37oc, respectively. platelet aggregation studies show that purified lao inhibited adp-induced platelet aggregation dose-dependently at 0.01 to 0.1 ¦Ìm with 50% inhibitory concentration (ic50) of 0.04 ¦Ìm, whereas at a 0.08 ¦Ìm concentration it did not induce appreciable aggregation on normal platelet-rich plasma (prp). the purified protein catalyzed oxidative deamination of l-amino acids while the most specific substrate was l-leucine. the purified lao oxidizes only l-forms, but not d-forms of amino acids, to produce h2o2. the enzyme is important for the purification and determination of certain amino acids and for the preparation of ¦Á-keto acids.
%K l-amino acid oxidase
%K bungarus caeruleus
%K platelet aggregation.
%U http://www.scielo.br/scielo.php?script=sci_abstract&pid=S1678-91992010000100007&lng=en&nrm=iso&tlng=en