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Samson MR, Klis FM, Homan WL, et al. Composition and properties of the sexual agglutinins of the flagellated green alga Chlamydomonas eugametos. Planta. 1987;170(3):314-21doi: 10.1007/BF00395022.
Samson, M. R., Klis, F. M., Homan, W. L., van Egmond, P., Musgrave, A., & van den Ende, H. (1987). Composition and properties of the sexual agglutinins of the flagellated green alga Chlamydomonas eugametos. Planta, 170(3), 314-21. https://doi.org/10.1007/BF00395022
Samson, M R, et al. "Composition and properties of the sexual agglutinins of the flagellated green alga Chlamydomonas eugametos." Planta vol. 170,3 (1987): 314-21. doi: https://doi.org/10.1007/BF00395022
Samson MR, Klis FM, Homan WL, van Egmond P, Musgrave A, van den Ende H. Composition and properties of the sexual agglutinins of the flagellated green alga Chlamydomonas eugametos. Planta. 1987 Mar;170(3):314-21. doi: 10.1007/BF00395022. PMID: 24232960.
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Planta. 1987 Mar;170(3):314-21. doi: 10.1007/BF00395022.

Composition and properties of the sexual agglutinins of the flagellated green alga Chlamydomonas eugametos.

Planta

M R Samson, F M Klis, W L Homan, P van Egmond, A Musgrave, H van den Ende

Affiliations

  1. Department of Plant Physiology, University of Amsterdam, Kruislaan 318, NL-1098 SM, Amsterdam, The Netherlands.

PMID: 24232960 DOI: 10.1007/BF00395022

Abstract

Sexual interaction between gametes of opposite mating type (mt) of the unicellular green alga Chlamydomonas eugametos starts with agglutination of the cells via particular glycoproteins on the flagellar surface. Purification of these socalled agglutinins was achieved by a three-step procedure consisting of, successively, gel filtration, anion-exchange chromatography, and high-performance gel filtration. The amino-acid and sugar compositions of both agglutinins showed a high degree of similarity; the most prominent amino acids were hydroxyproline, serine and glycine, and the main sugars were arabinose and galactose. The carbohydrate portions represented about half of the molecular mass of both agglutinins. Using high-performance gel filtration, a calibration curve was constructed for high-molecular-mass compounds from which the Stokes' radius of the sexual agglutinins could be estimated. The mt (+) agglutinin had a Stokes' radius of 39 nm and a sedimentation coefficient of 9.3 S. From these data its molecular mass was estimated to be 1.2·10(6). The corresponding data for the mt (-) agglutinin were 38 nm, 9.7 S and 1.3·10(6), respectively. The biological activity of both agglutinins was destroyed by mild periodate treatment. Treatment with specific glycosidases had a differential effect on the biological activity of the agglutinins. These observations indicate that carbohydrate side-chains are needed for biological activity and perhaps are responsible for the specifity of the sexual agglutinins. A comparison of both agglutinins is given and their possible structure is discussed in relation to their amino-acid and sugar compositions.

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