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  • Flagella  (4)
  • Glycoprotein  (3)
  • 1995-1999
  • 1985-1989  (2)
  • 1980-1984  (5)
  • 1935-1939
  • 1
    ISSN: 1432-2048
    Keywords: Chlamydomonas (gametes) ; Flagellum (mating type) ; Glycoprotein ; Sexual agglutination (gametes)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Gametes of opposite mating type (mt + and mt -) of the green alga Chlamydomonas eugametos agglutinate via their flagella as a prelude to sexual fusion. To quantitate sexual agglutination, an in vitro assay has been developed using 35S-labeled flagella and the isolated mt -agglutination factor. It is shown that not only isolated flagella, but also the mt -agglutination factor rapidly bind to the flagella of intact gametes of the opposite mating type. This confirms the role of the mt -agglutination factor in determining the sexual agglutinability of mt -gametes. As a function of binding, the agglutinative power of the flagella of both mating types is destroyed by a temperature-sensitive process. Likewise, the mt -agglutination factor can be completely inactivated.
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  • 2
    ISSN: 1432-2048
    Keywords: Chlamydomonas (agglutination) ; Flagellum ; Glycoprotein ; Membrane barrier
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Evidence is presented which supports the concept of a functional membrane barrier in the transition zone at the base of each flagellum of Chlamydomonas eugametos gametes. This makes it unlikely that agglutination factors present on the surface of the cell body can diffuse or be transported to the flagellar membrane. The evidence is as follows: 1) The glycoprotein composition of the flagellar membrane is very different to that of the cell-body plasma membrane. 2) The flagella of gametes treated with cycloheximide, tunicamycin or α, α′-dipyridyl become non-agglutinable but the source of agglutination factors on the cell body is not affected. 3) Even under natural conditions when the flagella are non-agglutinable, for example in vis-à-vis pairs or in appropriate cell strains that are non-agglutinable in the dark, the cell bodies maintain the normal complement of active agglutinins. 4) When flagella of living cells are labeled with antibodies bound to fluorescein, the label does not diffuse onto the cell-body surface. 5) When gametes fuse to form vis-à-vis pairs, the original mating-type-specific antigenicity of each cell body is slowly lost (probably due to the antigens diffusing over both cell bodies), while the specific antigenicity of the flagellar surface is maintained. Even when the flagella of vis-à-vis pairs are regenerated from cell bodies with mixed antigenicity, the antigenicity of the flagella remains matingtype-specific. 6) Evidence is presented for the existence of a pool of agglutination factors within the cell bodies but not on the outer surface of the cells.
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  • 3
    ISSN: 1432-072X
    Keywords: Chlamydomonas ; Agglutination ; Flagella ; Glycoproteins ; Anti-PAS-1.2 serum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Chlamydomonas eugametos gametes agglutinate sexually by their flagellar surfaces. The agglutination factor on mating type minus (mt-) gametes is thought to be a glycoprotein named PAS-1.2. To test this idea, an antiserum was raised against purified PAS-1.2., which reacted with isolated PAS-1.2 (immunoprecipitation tests) and blocked the ability of isolated PAS-1.2 to induce sexual twitching in mt + gametes. When tested with living cells, the antiserum specifically agglutinated mt - gametes and induced a reaction resembling twitching. Mt + flagella were shown to bind the antiserum (indirect immunofluorescence) but much less than mt - gametes. Mt - gametes pretreated with Fab fragments of the antiserum were unable to reproduce sexually, while treated mt + gametes were unaffected. This effect presumably results from the ability of the serum to block mt - sexual agglutination, for mt - isoagglutinin was completely inactivated by the serum, while mt + isoagglutinin was unaffected. It is therefore argued that PAS-1.2 is the in vivo mt - agglutination factor. However it is shown that the antiserum was able to react in vitro not only with PAS-1.2 but with several other proteins in both mt - and mt + flagella.
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  • 4
    ISSN: 1432-072X
    Keywords: Chlamydomonas ; Sexual reproduction ; Agglutination ; Flagella ; Antigenic determinant ; Glycoproteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A labeled oligosaccharide fraction, obtained by reductive β-elimination of an extract of minus mating-type flagella of Chlamydomonas eugametos, is shown to contain a disaccharide fraction which is bound by an antiserum raised against the sexual agglutination factor present at the flagellar surface of that species. The fraction contains arabinose and galactose. It is argued that galactose and/or arabinose may be a functional constituent of the agglutination factor.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 126 (1980), S. 77-81 
    ISSN: 1432-072X
    Keywords: Chlamydomonas ; Sex ; Flagella ; Agglutination ; Glycoproteins ; Immunochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract To identify mating type-specific glycoproteins associated with the flagellar membrane of Chlamydomonas eugametos, which could be involved in sexual agglutination, antibodies were raised in rabbits against purified gamete flagella of either mating type. The immunoglobulin (Ig) fractions exhibited partial mating-type specificity in agglutinating gametes, in the indirect immunofluorescence test and in the crossed immunoelectrophoresis test. This specificity was strongly enhanced by absorbing the fractions with flagella of the opposite mating type. Absorbed Ig fractions produced a single precipitation line with Triton extracts of gamete flagella in the crossed immunoelectrophoresis technique. On polyacrylamide gel electrophoresis this line appeared to contain two flagellar glycoprotein fractions, PAS 1 and PAS 4. Polyacrylamide gels of flagellar extracts incubated with these Ig fractions, followed by staining with peroxidase-anti-rabbit Ig resulted in the staining of only the PAS 1 and PAS 4 bands, which confirms that these components of the flagellar membrane are mating type-specific antigens.
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  • 6
    ISSN: 1432-2048
    Keywords: Chlamydomonas ; Glycoprotein ; Monoclonal antibody ; Sugar (O-methylated)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Monoclonal antibodies are described that are directed against cell surface components of the unicellular green alga Chlamydomonas eugametos. These antibodies recognize strain-specific epitopes which occur at the surface of vegetative and gametic cells. Two different groups of epitopes are distinguished that are never detectable together in one clonal cell culture. Evidence is presented showing that the antigenicity of cell surface molecules is a consequence of the presence of particular O-methylated sugars. Monoclonal antibodies reacting with one group of epitopes were studied in more detail, and immunoprecipitation and Western-blot studies showed that these epitopes can be arranged into four classes. The use of these monoclonal antibodies as strain-specific markers in light- and electron-microscopical techniques is illustrated.
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  • 7
    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.
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