Preparation and purification of soybean lipoxygenase-derived unsaturated hydroperoxy and hydroxy fatty acids and determination of molar absorptivities of hydroxy fatty acids

Graff, Gustav; Anderson, L. A.; Jaques, Larry W.

doi:10.1016/0003-2697(90)90525-e

Cited by 90 publications

(48 citation statements)

References 12 publications

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“…This was possibly due to improper positioning 12(S)-HPETE determined by this method was within error of the published values by Graff et al, after correcting for differences in solvent conditions ( 36 ). Kinetic assays were carried out in 25 mM HEPES buffer (pH 7.5) with substrate concentrations ranging from 1 M to 20 M, and they were initiated by the addition of enzyme (approximately 20 nM 12-LOX).…”

Section: -Lox Product Identifi Cation and Distributionsupporting

confidence: 51%

Investigations of human platelet-type 12-lipoxygenase: role of lipoxygenase products in platelet activation

Ikei

Yeung

Apopa

et al. 2012

Journal of Lipid Research

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Section: -Lox Product Identifi Cation and Distributionsupporting

confidence: 51%

Investigations of human platelet-type 12-lipoxygenase: role of lipoxygenase products in platelet activation

Ikei

Yeung

Apopa

et al. 2012

Journal of Lipid Research

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“…[9], with minor modifications (i.e. lipoxygenase was added in three aliquots to the reaction mixture with vigorous shaking) as suggested by Graft et al [28].…”

Section: Methodsmentioning

confidence: 99%

A stress‐associated citrus protein is a distinct plant phospholipid hydroperoxide glutathione peroxidase

et al. 1995

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A protein whose level is markedly increased upon exposure of cultured citrus cells and whole plants to NaCI, was shown to specifically catalyze the reduction of phosphatidylcboHne hydroperoxide in the presence of glutathione. This enzymatic activity was shown to be independent of a similar activity exhibited by glututhione $-transferase in plants. This finding corroborates the significant homology (52%) accounted between the deduced amino acid sequence o¢ the gene encoding for this protein and that of mammalian phosphollpld hydroperoxide glutathlone peroxidases. While the mammalian enzyme is known and well investigated, this study estubllshes the presence of this key protein also in plants.

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“…The cistrans conjugated hydro(pero)xy fatty acids were assumed to have an extinction coefficient of 25,000 cm 21 M 21 (27). Lipoxygenase activity was monitored by ultraviolet (UV) spectroscopy (235-237 nm) in 0.1 M NaBO 3 buffer (pH 9.0) with 50-120 mM substrate.…”

Section: Mn-lox Assaymentioning

confidence: 99%

Factors influencing the rearrangement of bis-allylic hydroperoxides by manganese lipoxygenase

Oliw

2008

Journal of Lipid Research

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Manganese lipoxygenase (Mn-LOX) catalyzes the rearrangement of bis-allylic S-hydroperoxides to allylic Rhydroperoxides, but little is known about the reaction mechanism. 1-Linoleoyl-lysoglycerophosphatidylcholine was oxidized in analogy with 18:2n-6 at the bis-allylic carbon with rearrangement to C-13 at the end of lipoxygenation, suggesting a "tail-first" model. The rearrangement of bisallylic hydroperoxides was influenced by double bond configuration and the chain length of fatty acids. The Gly316Ala mutant changed the position of lipoxygenation toward the carboxyl group of 20:2n-6 and 20:3n-3 and prevented the bis-allylic hydroperoxide of 20:3n-3 but not 20:2n-6 to interact with the catalytic metal. The oxidized form, Mn III -LOX, likely accepts an electron from the bis-allylic hydroperoxide anion with the formation of the peroxyl radical, but rearrangement of 11-hydroperoxyoctadecatrienoic acid by Mn-LOX was not reduced in D 2 O (pD 7.5), and aqueous Fe 31 did not transfer 11S-hydroperoxy-9Z,12Z,15Z-octadecatrienoic acid to allylic hydroperoxides. Mutants in the vicinity of the catalytic metal, Asn466Leu and Ser469Ala, had little influence on bis-allylic hydroperoxide rearrangement. In conclusion, Mn-LOX transforms bis-allylic hydroperoxides to allylic by a reaction likely based on the positioning of the hydroperoxide close to Mn 31 and electron transfer to the metal, with the formation of a bis-allylic peroxyl radical, b-fragmentation, and oxygenation under steric control by the protein.-Oliw, E. H. Factors influencing the rearrangement of bis-allylic hydroperoxides by manganese lipoxygenase. J. Lipid Res. 2008. 49: 420-428.

show abstract

Preparation and purification of soybean lipoxygenase-derived unsaturated hydroperoxy and hydroxy fatty acids and determination of molar absorptivities of hydroxy fatty acids

Cited by 90 publications

References 12 publications

Investigations of human platelet-type 12-lipoxygenase: role of lipoxygenase products in platelet activation

Investigations of human platelet-type 12-lipoxygenase: role of lipoxygenase products in platelet activation

A stress‐associated citrus protein is a distinct plant phospholipid hydroperoxide glutathione peroxidase

Factors influencing the rearrangement of bis-allylic hydroperoxides by manganese lipoxygenase

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