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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

Synonym(s):

Linoleate:oxygen oxidoreductase, Lipoxygenase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type V

Quality Level

form

ammonium sulfate suspension

specific activity

500,000-1,000,000 units/mg protein

mol wt

94 kDa

storage temp.

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).

Biochem/physiol Actions

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

Unit Definition

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.

Physical form

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

Preparation Note

Prepared by ion exchange chromatography and hydrophobic interaction chromatography.

Analysis Note

Protein determined by biuret.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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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