octadecadienoic acid/soia

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Hydroperoxide Lyase and Other Hydroperoxide-Metabolizing Activity in Tissues of Soybean, Glycine max.

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Hydroperoxide lyase (HPLS) activity in soybean (Glycine max) seed/seedlings, leaves, and chloroplasts of leaves required detergent solubilization for maximum in vitro activity. On a per milligram of protein basis, more HPLS activity was found in leaves, especially chloroplasts, than in seeds or

Catalytic characterization of heterodimeric linoleate 13S-lipoxygenase from black soybean (Glycine max (L.) Merr.)

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A novel lipoxygenase (BLOX) was purified from black soybean (Glycine max (L.) Merr.), and its catalytic properties were characterized. The molecular weight of BLOX was 101 kDa and its unique heterodimeric structure with two different subunits of molecular weight 46 kDa and 55 kDa was elucidated. The

Expanding resolution of metalloprotein separations from soybean seeds using 2D-HPLC-ICP-MS and SDS-PAGE as a third dimension.

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This work reports on the use of a three dimensional separation system to enhance metalloprotein information when considering soybean seeds. Separations using size exclusion chromatography (SEC) allowed identification of three metal fractions. Following an anion exchange (AEX) chromatographic

Appearance of new lipoxygenases in soybean cotyledons after germination and evidence for expression of a major new lipoxygenase gene.

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The appearance and subsequent disappearance of lipoxygenase activity at pH 6.8 in germinated cotyledons of soybean (Glycine max [L.]) was shown using a variant soybean cultivar (Kanto 101) that lacks the two lipoxygenase isozymes, L-2 and L-3, that are present in dry seeds of a normal soybean

Soybean lipoxygenase-1 oxidizes 3Z-nonenal. A route to 4s-hydroperoxy-2e-nonenal and related products

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In previous work with soybean (Glycine max), it was reported that the initial product of 3Z-nonenal (NON) oxidation is 4-hydroperoxy-2E-nonenal (4-HPNE). 4-HPNE can be converted to 4-hydroxy-2E-nonenal by a hydroperoxide-dependent peroxygenase. In the present work we have attempted to purify the

Characterization of a C-5,13-Cleaving Enzyme of 13(S)-Hydroperoxide of Linolenic Acid by Soybean Seed.

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An activity was found in mature soybean seeds (Glycine max L. cv Century) that cleaved 13(S)-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid (13S-HPOT) into 13-oxo-9(Z),11(E)-tridecadienoic acid and two isomeric pentenols, 2(Z)-penten-1-ol and 1-penten-3-ol. Isomeric pentene dimers were also

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