Isolation of monovalent sexual binding components from Chlamydomonas eugametos flagellar membranes
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Several treatments were tested to extract the sexual binding site from membrane vesicles derived from the flagellar surface of Chlamydomonas eugametos. Extraction with detergents, chaotropic and hydrogen bond-disrupting agents, as well as sonication, was effective in reducing the isoagglutination activity of these membrane vesicles. Complementary with this reduction, a sex-specific biological activity related to isoagglutination, called “twitch activity” appeared in the extract. This was only observed with vesicles derived from minus mating type (mt-) gametes. After fractionation of the extract, one high-molecular weight glycoprotein fraction appeared to be responsible for this activity. When extracts were treated with cross-linking agents, a pelletable fraction was obtained with isoagglutinative activity. We conclude that the mt- factor, responsible for twitch activity, causes isoagglutination when it is rendered multivalent.
Key wordsChlamydomonas Sex Isoagglutination Membrane vesicles Glycoproteins Cell interaction
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