Purification and partial characterization of an l-amino acid oxidase from bushmaster snake (Surucucu pico de jaca) Lachesis muta venom
Braz. j. med. biol. res
;
24(3): 249-60_, mar. 1991. tab
Article
in English
| LILACS
| ID: lil-99563
RESUMO
L-amino-acid oxidase(L-AO) form the venom of Lachesi muta muta was purified 72 times (38%) by gel filtration on Sephadex G-100, followed by ion exchange chromatography on DEAE-cellulose and gel filtration on Sephacryl S-300. The protein was shown to be homogeneous by polyacrylamide gel electroforesis, immunoelectrophoresis, immunodiffusion and isoelectric focusing. Its specific activity was 44.4 units/mg protein, using 7.5 mM L-leucine as substrate a nd O-dianisidine as electron donor,at pH 7.6 and 25§C. The increase in absorbance at 436 nm was recorded. The enzyme was characterized as a glycoprotein with an S20,w=6.72,MW=138,000 and pI=5.2. It presented maxima at 389 and 460 nm and contained 2 mol of FAD per mole protein
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Index:
LILACS (Americas)
Main subject:
Snakes
/
Crotalid Venoms
/
Amino Acid Oxidoreductases
Limits:
Animals
Language:
English
Journal:
Braz. j. med. biol. res
Journal subject:
Biology
/
Medicine
Year:
1991
Type:
Article
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