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  • Phytohemagglutinin  (1)
  • amino acid sequences  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Detection and characterization of a lectin from non-seed tissue ofPhaseolus vulgaris (1984)
    Springer
    Planta 161 (1984), S. 223-228 
    Details
    ISSN: 1432-2048
    Keywords: Lectin (vegetative tissue) ; Phaseolus (lectin) ; Phytohemagglutinin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The distribution of lectin in various tissues ofPhaseolus vulgaris L. (cv. red) has been investigated using a sensitive solid-phase enzyme immunoassay. Roots, leaves and stems from 3- to 4-week-old plants were screened for their lectin content; low levels could be detected in all organs, with a relative distribution of 37% in roots, 20% in leaves and 43% in stems. The lectin from stemsleaves and roots was then isolated from 5- to 6-week-old plants using extraction, salt fractionation and affinity chromatography on immobilized porcine thyroglobulin. A comparative study of the seed lectin and the lectin isolated from 5- to 6-week-old plants was made using hemagglutination, inhibition of hemagglutination, immunodiffusion, polyacrylamide and agarose electrophoresis. The results showed that lectin isolated from the different tissues was immunologically identical and exhibited the same subunit structure and similar isolectin composition as the seed lectin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00982916
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  • 2
    Electronic Resource
    Electronic Resource
    Structure-function relationships amongLathyrus lectins (1987)
    Springer
    Glycoconjugate journal 4 (1987), S. 371-378 
    Details
    ISSN: 1573-4986
    Keywords: Lathyrus lectin/isolectins ; structure-function relationship ; amino acid sequences ; blood group specificity ; inhibition by sugars ; interaction with hman serum glycoproteins ; mitogenicity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The structure-function relationship of eight structurally very similarLathyrus lectins, which are two-chain lectins from theVicieae tribe, has been studied. Hemagglutination activity, inhibition of hemagglutination, glycoprotein reactivity and mitogenic activity were determined for each of the lectins. Despite the close structural resemblance, marked differences in the carbohydrate binding activity of theLathyrus lectins were recorded. These functional differences were related to small conformational changes due to minor differences in amino acid sequence of eachLathyrus lectin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01048370
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    Paper (German National Licenses)
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