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Merck

L6632

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:
9029-60-1
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-853-1
MDL number:
MFCD00131527
EC Number:
1.13.11.12 (BRENDA, IUBMB)

Key Documents

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Product Name

Lipoxidase from Glycine max (soybean), Type V, ammonium sulfate suspension, 500,000-1,000,000 units/mg protein

type

Type V

form

ammonium sulfate suspension

specific activity

500,000-1,000,000 units/mg protein

mol wt

94 kDa

storage temp.

2-8°C

Quality Level

200

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Analysis Note

Protein determined by biuret.

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.

Other Notes

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.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
SLCH5895
SLCC4512
SLBT2845
091K7026
070H7218

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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
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.
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
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
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
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