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s methyl l cysteine sulfoxide/allium
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Biosynthesis of s-methyl-L-cysteine and s-methyl-L-cysteine sulfoxide from methionine in garlic.
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Purification and Characterization of a C-S-Lyase from Ramson, the Wild Garlic,Allium ursinum.
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A C-S-lyase preparation from ramson, ALLIUM URSINUM L., has been purified to apparent homogeneity. Separation techniques applied were hydrophobic interaction chromatography, anion exchange chromatography, and gel permeation chromatography. A 52-fold purification was obtained. The enzyme could be
Isolation and Identification of Homologues of Ajoene and Alliin from Bulb-Extracts of Allium ursinum.
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From the chloroform extract of ALLIUM URSINUM L. (Liliaceae) bulbs, in addition to other sulfur-containing constituents ( E/Z)-4,5,9-trithiadeca-1,6,11-dien-9-oxide [= methylajoene) and ( E/Z)-4,5,9-trithiaocta-1,6-dien-9-oxide (= dimethylajoene) were isolated and identified by NMR and mass
HPLC of S-Alk(en)yl-L-cysteine Derivatives in Garlic including Quantitative Determination of (+)-S-Allyl-L-cysteine Sulfoxide (Alliin).
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Methods developed for the separation of S-alk(en)yl- L-cysteines and their corresponding (+/-)-sulfoxide isomers by reversed-phase HPLC were applied to the analysis of various garlic samples including fresh garlic, dried extracts, and garlic preparations. Extracts were chromatographed following
A novel amino acid glycoside and three amino acids from Allium sativum.
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A novel amino acid glycoside (-)-N-(1'-deoxy-1'-beta-D-fructopyranosyl)-S-allyl-L-cysteine sulfoxide [1], was isolated from a hydrophilic extract of the leaves of Allium sativum (Alliaceae), together with three known compounds: (+)-S-allyl-L-cysteine sulfoxide [2],(+)-S-methyl-L-cysteine sulfoxide
Cysteine sulfoxides and alliinase activity of some Allium species.
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The flavor precursors of 17 species belonging to the Alliaceae family were analyzed by HPLC, and results were evaluated with respect to the classification of species into their genus, subgenus, and section. Identification and quantification of these precursors were carried out by synthetic and
On the Isolation and Characterization of a C-S-Lyase Preparation from Leek,Allium porrum.
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The C-S-lyase protein from leek, ALLIUM PORRUM L., has been purified and characterized. The molecular mass of the native protein was determined with M (r) = 100 000, including two similar subunits, M (r) = 50 000. The tendency of the native protein to form a trimer, M (r) = 300 000, could be
Characterization of some Allium hybrids by aroma precursors, aroma profiles, and alliinase activity.
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Various Allium hybrids, obtained by the crossbreeding of Allium cepa (onion) as the mother plant and six taxonomically distant wild species obtained by embryo rescue, were investigated with special respect to their individual profiles of cysteine sulfoxides as well as enzymically and nonenzymically
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