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  • Agglutination (sexual)  (1)
  • Agglutination factor  (1)
  • 1980-1984  (2)
  • 1955-1959
  • 1940-1944
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Planta 153 (1981), S. 362-369 
    ISSN: 1432-2048
    Keywords: Agglutination (sexual) ; Chlamydomonas ; Flagella ; Glycoprotein and sexual agglutination ; Membrane ; Sexual reproduction (Chlamydomonas)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Chlamydomonas eugametos gametes can sexually agglutinate via their flagellar surfaces whereas vegetative cells cannot. Therefore, flagellar glycoproteins, present in gamete cells but absent from vegetative cells, were investigated as prospective mt -agglutination factors. They were identified as periodic acid Schiff (PAS) stained bands separated in sodium dodecyl sulphate-polyacrylamide electrophoresis gels. Gamete-specific bands were determined by comparison with equivalent gels of vegetative flagella and by immunological techniques using antisera raised against isolated mt - gamete flagella. Four high molecular weight flagellar glycoproteins proved to be gamete specific (PAS-1.2, PAS-1.3, PAS-3 and PAS-4). They were extracted from flagella by 3 M guanidine thiocyanate, separated in a column of Sepharose 2B, and tested for in vitro agglutination activity on mt + gametes. A single peak of activity was found to be correlated with the presence of the PAS-1.2 band. It is shown that mt - agglutination activity is related to the concentration of this glycoprotein in flagellar membranes.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: Agglutination factor ; Chlamydomonas ; (Iso) agglutination ; Sexual reproduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Gametes ofChlamydomonas eugametos produce membrane vesicles, called isoagglutinins, which are shed into the culture fluid. It is assumed that they originate from the flagellar membrane for, like flagella, they can bind to the flagellar surface of gametes of the opposite mating type (mt). The composition ofmt - isoagglutinin was investigated with respect to this agglutinability. When the agglutination factor present on the surface ofmt - isoagglutinins (PAS-1.2) was removed, together with other membrane bound glycoproteins, the membrane vesicles were rendered inactive. They could be reactivated however by incubation with the extracted glycoproteins in a time-and concentration-dependent manner. The agglutination factor proved to be necessary yet sufficient in itself for the reactivation process to occur. Experiments with CsCl density gradients showed that the agglutination factor truly bound to the vesicles during reactivation. Inactivated vesicles derived frommt + gametes could be reactivated to gainmt - properties. Reactivation was inhibited by prior treatment with trypsin. The results indicate that the agglutination factor inmt - isoagglutinins is an extrinsic membrane protein bound to an intrinsic proteinaceous receptor.
    Type of Medium: Electronic Resource
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