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Archives of Microbiology

, Volume 128, Issue 1, pp 120–125 | Cite as

Isolation of monovalent sexual binding components from Chlamydomonas eugametos flagellar membranes

  • W. L. Homan
  • A. Musgrave
  • E. M. Molenaar
  • H. van den Ende
Article

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.

Key words

Chlamydomonas Sex Isoagglutination Membrane vesicles Glycoproteins Cell interaction 

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Copyright information

© Springer-Verlag 1980

Authors and Affiliations

  • W. L. Homan
    • 1
  • A. Musgrave
    • 1
  • E. M. Molenaar
    • 1
  • H. van den Ende
    • 1
  1. 1.Department of Plant PhysiologyUniversity of AmsterdamAmsterdamThe Netherlands

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