L6632
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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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-853-1
MDL number:
Numéro CE :
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Laissez-nous vous aiderNom du produit
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
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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.
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.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Classe de stockage
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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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
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.
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
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
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