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Key Documents

A9253

Sigma-Aldrich

L-Amino Acid Oxidase from Crotalus adamanteus

Type I (dried venom)

Synonyme(s) :

L-AAO, L-Amino acid: oxygen oxidoreductase (deaminating)

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

Crotalus adamanteus

Niveau de qualité

Type

Type I (dried venom)
Type I

Forme

powder

Poids mol.

~130 kDa

Solubilité

H2O: soluble 1.0 mg/mL, clear(lit.)

Température de stockage

−20°C

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Description générale

L-Amino acid oxidase (LAAO) is a flavoprotein with a molecular weight of 130 kDa. It consists of two different subunits of approximately 70 kDa. Each molecule of holoenzyme has two flavin adenine dinucleotide (FAD) molecules. LAAO is a glycoprotein containing about 2-5% carbohydrate, including sialic acid. optimum pH is approximately 7.5. It occurs in many snake venoms apart from microorganisms and animal tissue, especially in kidney. In the N-terminal region, it has a βαβ domain with glutamic acid residues. LAAO imparts yellow color to venom.

Application

L-Amino Acid Oxidase from Crotalus adamanteus has been used in the quantification of rid protein in imine deaminase activity.
L-amino acid oxidase (LAAO) is used to convert L-amino acids to their corresponding α-keto acids. L-amino acid oxidase, from Sigma, has been used in leucine aminopeptidase (LAP) activity assays. The enzyme has been immobilized and used in an enzymatic flow-injection procedure with chemiluminescence detection for on-site determination of L-alanine.

Actions biochimiques/physiologiques

L-Amino acid oxidase (LAAO) from Crotalus adamanteus requires Mg2+ for its activation. The N-terminal region is essential for FAD binding. The H2O2 generated by LAAO based oxidation reactions lead to prevention of platelet aggregation and induces edema and apoptosis. LAAO activity is inhibited by ethylenediaminetetraacetic acid (EDTA) and phenylmethylsulfonyl fluoride (PMSF).

Notes préparatoires

Dissolves in water at 1 mg/mL concentration to form a clear solution.

Pictogrammes

Skull and crossbones

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

Acute Tox. 1 Inhalation - Acute Tox. 2 Dermal - Acute Tox. 2 Oral

Code de la classe de stockage

6.1A - Combustible acute toxic Cat. 1 and 2 / very toxic hazardous materials

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Glycerol-induced development of catalytically active conformation of Crotalus adamanteus L-amino acid oxidase in vitro
Raibekas AA and Massey V
Proceedings of the National Academy of Sciences of the USA, 93(15), 7546-7551 (1996)
Alba Martín-Barreiro et al.
Analytical and bioanalytical chemistry, 414(8), 2641-2649 (2022-01-23)
An enzymatic-colorimetric method has been developed based on the reaction between L-phenylalanine (L-Phe) and the L-amino acid oxidase (LAAO) in the presence of Au(III), which has led to the formation of gold nanoparticles. The intensity of the localized surface plasmon
Characterization of L-amino Acid Oxidase Derived from Crotalus adamanteus Venom: Procoagulant and Anticoagulant Activities
Nielsen VG
International Journal of Molecular Sciences, 20(19), 4853-4853 (2019)
The venom-gland transcriptome of the eastern diamondback rattlesnake (Crotalus adamanteus)
Rokyta DR, et al.
BMC Genomics, 13(1), 312-312 (2012)
Crystalline L-amino acid oxidase of Crotalus adamanteus
Wellner D and Meister A
The Journal of Biological Chemistry, 235(7), 2013-2018 (1960)

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