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Isolation of monovalent sexual binding components from Chlamydomonas eugametos flagellar membranes

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Abstract

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.

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Authors and Affiliations

  1. Department of Plant Physiology, University of Amsterdam, Kruislaan 318, Amsterdam, The Netherlands

    W. L. Homan, A. Musgrave, E. M. Molenaar & H. van den Ende

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  1. W. L. Homan
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  2. A. Musgrave
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  3. E. M. Molenaar
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  4. H. van den Ende
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Homan, W.L., Musgrave, A., Molenaar, E.M. et al. Isolation of monovalent sexual binding components from Chlamydomonas eugametos flagellar membranes. Arch. Microbiol. 128, 120–125 (1980). https://doi.org/10.1007/BF00422315

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  • DOI: https://doi.org/10.1007/BF00422315

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