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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 67 (2002), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A capillary electrophoresis method was developed for the chiral separation of D-L valine, isoleucine, and leucine. The separation of derivatized amino acids with 9-fluorenylmethyl-chloroformate was performed by micellar electrokinetic capillary chromatography. We optimized the method by varying β-cyclodextrin and sodium dodecyl sulphate concentrations in the presence of 2-propanol. The proposed method was applied to the determination of D-forms of valine, Isoleucine, and leucine in the presence of an excess of relative L forms, in commercial supplements for sport nutrition. Results demonstrated that the separation of enantiomers was possible up to an enantiomeric ratio of 1:100. The analysis of selected products confirmed the enantiomeric purity of utilized amino acids.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-9104
    Keywords: Amino acids ; Celiac disease ; Cells ; Cereals ; Prolamines ; Quinoa seeds
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract The edible seeds of the quinoa plant contain small quantities of alcohol-soluble protein which, after peptic-tryptic digestion, are unable to agglutinate K562(s) cells. When separated by affinity chromatography on sepharose-6B coupled with mannan, peptic-tryptic digest separated in two fractions. Fraction B peptides (about 1% of total protein) were shown to agglutinate K562(s) cells at a very low concentration, whereas peptides in fraction A and in the mixed fraction A+B were inactive, suggesting that fraction A contains protective peptides that interfere with the agglutinating activity of toxic peptides in fraction B.
    Type of Medium: Electronic Resource
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