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L6632

Sigma-Aldrich

Lipoxidase from Glycine max (soybean)

Type V, ammonium sulfate suspension, 500,000-1,000,000 units/mg protein

Synonyme(s) :

Linoleate:oxygen oxidoreductase, Lipoxygenase

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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

Type

Type V

Forme

ammonium sulfate suspension

Activité spécifique

500,000-1,000,000 units/mg protein

Poids mol.

94 kDa

Température de stockage

2-8°C

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Application

Lipoxidase, or lipoxygenase, from Glycine max (soybean) has been used for the modification of low density lipoprotein, isolated from human plasma.
The soybean enzyme will use arachidonic acid as a substrate, with ~ 15% of the activity indicated using linoleic acid as the substrate; the product of arachidonic acid oxidation is 12- or 15-hydroperoxyarachidonic acid (12-HPETE or 15-HPETE).

Actions biochimiques/physiologiques

Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.

Définition de l'unité

One unit will cause an increase in A234 of 0.001 per min at pH 9.0 at 25 °C when linoleic acid is the substrate in 3.0 ml volume (1 cm light path). One A234 unit is equivalent to the oxidation of 0.12 μmole of linoleic acid.

Forme physique

Suspension in 2.3 M (NH4)2SO4 solution, pH approx. 6.0

Notes préparatoires

Prepared by ion exchange chromatography and hydrophobic interaction chromatography.

Remarque sur l'analyse

Protein determined by biuret.

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Aldana M Ramirez et al.
Lipids, 48(10), 1005-1015 (2013-07-31)
The lipid precursor alcohols of pyrethrins-jasmolone, pyrethrolone and cinerolone-have been proposed as sharing parts of the oxylipin pathway with jasmonic acid. This implies that one of the first committed steps of pyrethrin biosynthesis is catalyzed by a lipoxygenase, catalyzing the
Nisreen Faizo et al.
Foods (Basel, Switzerland), 10(2) (2021-02-07)
Lipid peroxides (LOOHs) abound in processed food and have been implicated in the pathology of diverse diseases including gut, cardiovascular, and cancer diseases. Recently, RNA Sequencing (RNA-seq) has been widely used to profile gene expression. To characterize gene expression and
P Harduin et al.
Journal of lipid research, 36(5), 919-930 (1995-05-01)
We studied the effect of in vitro moderate oxidation on low density lipoprotein (LDL) conformation and metabolism. LDL was modified with either copper ions or phospholipase A2 plus lipoxygenase and, in both cases, mild oxidative conditions were used. The resulting
Marc P Baggelaar et al.
Bioorganic & medicinal chemistry, 21(17), 5271-5274 (2013-07-23)
A catalytic asymmetric synthesis of (S)-(-)-zearalenone is reported using asymmetric allylic alkylation for the introduction of the stereocenter. (S)-(-)-Zearalenone turned out to be a novel lipoxygenase inhibitor.
E Wieland et al.
Proceedings of the National Academy of Sciences of the United States of America, 90(13), 5929-5933 (1993-07-01)
Oxidative modification of low density lipoprotein is believed to be an important pathway by which the lipoprotein becomes atherogenic. The in vitro systems for oxidative modification of low density lipoprotein thus far described all appear to depend upon the presence

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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