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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 68 (2003), 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: : We describe an ELISA assay to measure the active lectin content in dietary supplements containing protein extracts from Phaseolus vulgaris. Phytohemagglutinin (PHA) is known to induce serious consequences for metabolism and health when consumed raw or only lightly cooked. The ELISA was performed using plates preliminarily coated with porcine thyroglobulin, which has high specificity binding to active lectin. The bound active lectin was detected by a rabbit anti-PHA IgG and a secondary antibody enzyme conjugate. An assessment of linearity and analytical range were also performed. The data obtained showed good repeatability, specificity and a limit of quantification of 15 ng of PHA. The sensitivity of the method corresponds to 30 ppm.
    Type of Medium: Electronic Resource
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  • 2
    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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  • 3
    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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