Impairment of Platelet Aggregation by Echis colorata Venom Mediated by L-Amino Acid Oxidase or H2O2

SummaryEchis colorata bites cause impairment of platelet aggregation and hemostatic disorders. The mechanism by which the snake venom inhibits platelet aggregation was studied. Upon fractionation, aggregation impairment activity and L-amino acid oxidase activity were similarly separated from the crude venom, unlike other venom enzymes. Preparations of L-amino acid oxidase from E.colorata and from Crotalus adamanteus replaced effectively the crude E.colorata venom in impairment of platelet aggregation. Furthermore, different treatments known to inhibit L-amino acid oxidase reduced in parallel the oxidase activity and the impairment potency of both the venom and the enzyme preparation. H2O2 mimicked characteristically the impairment effects of L-amino acid oxidase and the venom. Catalase completely abolished the impairment effects of the enzyme and the venom. It is concluded that hydrogen peroxide formed by the venom L-amino acid oxidase plays a role in affecting platelet aggregation and thus could contribute to the extended bleeding typical to persons bitten by E.colorata.

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Platelet Aggregation and Antibacterial Effects of an L-Amino Acid Oxidase Purified from Bothrops alternatus Snake Venom.

ChemInform ◽

10.1002/chin.200436208 ◽

2004 ◽

Vol 35 (36) ◽

Author(s):

Rodrigo G. Stabeli ◽

Silvana Marcussi ◽

Guilherme B. Carlos ◽

Rosemeire C. L. R. Pietro ◽

Heloisa S. Selistre-de-Araujo ◽

...

Keyword(s):

Amino Acid ◽

Platelet Aggregation ◽

Snake Venom ◽

Acid Oxidase ◽

Antibacterial Effects ◽

Amino Acid Oxidase ◽

Bothrops Alternatus

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Platelet aggregation and antibacterial effects of an l-amino acid oxidase purified from Bothrops alternatus snake venom

Bioorganic & Medicinal Chemistry ◽

10.1016/j.bmc.2004.03.049 ◽

2004 ◽

Vol 12 (11) ◽

pp. 2881-2886 ◽

Cited By ~ 84

Author(s):

Rodrigo G. Stábeli ◽

Silvana Marcussi ◽

Guilherme B. Carlos ◽

Rosemeire C.L.R. Pietro ◽

Heloı́sa S. Selistre-de-Araújo ◽

...

Keyword(s):

Amino Acid ◽

Platelet Aggregation ◽

Snake Venom ◽

Acid Oxidase ◽

Antibacterial Effects ◽

Amino Acid Oxidase ◽

Bothrops Alternatus

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Molecular Cloning and Functional Analysis of Apoxin I, a Snake Venom-Derived Apoptosis-Inducing Factor withl-Amino Acid Oxidase Activity†

Biochemistry ◽

10.1021/bi992416z ◽

2000 ◽

Vol 39 (12) ◽

pp. 3197-3205 ◽

Cited By ~ 76

Author(s):

Shinichi Torii ◽

Kazuhiko Yamane ◽

Tetsuo Mashima ◽

Naomi Haga ◽

Kazuo Yamamoto ◽

...

Keyword(s):

Functional Analysis ◽

Amino Acid ◽

Molecular Cloning ◽

Snake Venom ◽

Oxidase Activity ◽

Acid Oxidase ◽

Amino Acid Oxidase ◽

Apoptosis Inducing Factor

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Purification and Characterization of Lupus Anticoagulant Like Protein from Agkistrodon Halys Brevicaudus Venom

Thrombosis and Haemostasis ◽

10.1055/s-0038-1650698 ◽

1996 ◽

Vol 76 (06) ◽

pp. 0993-0997

Author(s):

Zhao-Yan Li ◽

Xiao-Wei Wu ◽

Tie-Fu Yu ◽

Eric C-Y Lian

Keyword(s):

Amino Acid ◽

Lupus Anticoagulant ◽

Inhibitory Effect ◽

Clotting Factor ◽

Acid Oxidase ◽

Crude Venom ◽

Amino Acid Oxidase ◽

Sds Page ◽

The Individual ◽

Reducing Condition

SummaryBy means of CM-Sephadex C-25, DEAE-Sephadex A-50, Sephadex G-200, and Sephadex G-75 chromatographies, a lupus anticoagulant like protein (LALP) from Agkistrodon halys brevicaudus was purified. On SDS-PAGE, the purified LALP had a molecular weight of 25,500 daltons under non-reducing condition and 15,000 daltons under reducing condition. The isoelectric point was pH 5.6. Its N terminal amino acid sequencing revealed a mixture of 2 sequences: DCP(P/S)(D/G)WSSYEGH(C/R)Q(Q/K). It was devoid of phospho-lipaseA, fibrino(geno)lytic, 5′-nucleotidase, L-amino acid oxidase, phosphomonoesterase, phosphodiesterase and thrombin-like activities, which were found in crude venom. In the presence of LALP, PT, aPTT, and dRVVT of human plasma were markedly prolonged and its effects were concentration-dependent but time-independent. The inhibitory effect of LALP on the plasma clotting time was enhanced by decreasing phospholipid concentration in TTI test. The individual clotting factor activity was not affected by LALP when higher dilutions of LALP-plasma mixture were used for assay. Russell’s viper venom time was shortened when high phospholipid confirmatory reagent was used. Therefore, the protein has lupus anticoagulant property.

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Effect of hydrogen peroxide on d-amino acid oxidase from Rhodotorula gracilis

Enzyme and Microbial Technology ◽

10.1016/s0141-0229(00)00222-2 ◽

2000 ◽

Vol 27 (3-5) ◽

pp. 234-239 ◽

Cited By ~ 24

Author(s):

Isabel de la Mata ◽

Fernando Ramón ◽

Virginia Obregón ◽

Ma Pilar Castillón ◽

Carmen Acebal

Keyword(s):

Hydrogen Peroxide ◽

Amino Acid ◽

Acid Oxidase ◽

Amino Acid Oxidase ◽

Rhodotorula Gracilis

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The Effect of Castration and Testosterone Propionate on d-Amino Acid Oxidase Activity in the Mouse

Science ◽

10.1126/science.98.2534.89.a ◽

1943 ◽

Vol 98 (2534) ◽

pp. 89-89

Author(s):

L. C. Clark ◽

C. D. Kochakian ◽

R. Phyllis Fox

Keyword(s):

Amino Acid ◽

Oxidase Activity ◽

Testosterone Propionate ◽

Acid Oxidase ◽

Amino Acid Oxidase

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A new l -amino acid oxidase from Bothrops jararacussu snake venom: Isolation, partial characterization, and assessment of pro-apoptotic and antiprotozoal activities

International Journal of Biological Macromolecules ◽

10.1016/j.ijbiomac.2017.05.025 ◽

2017 ◽

Vol 103 ◽

pp. 25-35 ◽

Cited By ~ 19

Author(s):

Sante E.I. Carone ◽

Tássia R. Costa ◽

Sandra M. Burin ◽

Adélia C.O. Cintra ◽

Karina F. Zoccal ◽

...

Keyword(s):

Amino Acid ◽

Snake Venom ◽

Partial Characterization ◽

Acid Oxidase ◽

Amino Acid Oxidase ◽

Bothrops Jararacussu

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[218b] l-Amino acid oxidase (snake venom)

Metabolism of Amino Acids and Amines Part B - Methods in Enzymology ◽

10.1016/0076-6879(71)17105-4 ◽

1971 ◽

pp. 597-600 ◽

Cited By ~ 8

Author(s):

Daniel Wellner

Keyword(s):

Amino Acid ◽

Snake Venom ◽

Acid Oxidase ◽

Amino Acid Oxidase

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Nitroalkanes as Reductive Substrates for Flavoprotein Oxidases

Zeitschrift für Naturforschung B ◽

10.1515/znb-1972-0914 ◽

1972 ◽

Vol 27 (9) ◽

pp. 1052-1053 ◽

Cited By ~ 16

Author(s):

David J. T. Porter ◽

Judith G. Voet ◽

Harold J. Bright

Keyword(s):

Hydrogen Peroxide ◽

Amino Acid ◽

Glucose Oxidase ◽

Ph Dependence ◽

Kinetic Mechanism ◽

Acid Oxidase ◽

Amino Acid Oxidase ◽

Kinetics Of ◽

Oxidase Reaction ◽

Detailed Kinetic Mechanism

Nitroalkanes have been found to be general reductive substrates for D-amino acid oxidase, glucose oxidase and L-amino acid oxidase. These enzymes show different specificities for the structure of the nitroalkane substrate.The stoichiometry of the D-amino acid oxidase reaction is straightforward, consisting of the production of one mole each of aldehyde, nitrite and hydrogen peroxide for each mole of nitroalkane and oxygen consumed. The stoichiometry of the glucose oxidase reaction is more complex in that less than one mole of hydrogen peroxide and nitrite is produced and nitrate and traces of 1-dinitroalkane are formed.The kinetics of nitroalkane oxidation show that the nitroalkane anion is much more reactive in reducing the flavin than is the neutral substrate. The pH dependence of flavin reduction strongly suggests that proton abstraction is a necessary event in catalysis. A detailed kinetic mechanism is presented for the oxidation of nitroethane by glucose.It has been possible to trap a form of modified flavin in the reaction of D-amino acid oxidase with nitromethane from which oxidized FAD can be regenerated in aqueous solution in the presence of oxygen.

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