Cell wall glycoproteins from Chlamydomonas reinhardii,and their self-assembly |
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Authors: | J W Catt G J Hills K Roberts |
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Affiliation: | (1) John Innes Institute, Colney Lane, NR4 7UH Norwich, U.K.;(2) Present address: Fachbereich Biologie der Universität, Postfach 3049, D-6750 Karserslautern, Federal Republic of Germany |
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Abstract: | We have investigated the in vitro reassembly of the salt soluble, hydroxyproline rich, glycoproteins from the cell wall of Chlamydomonas reinhardii, into structured cell wall fragments. We have devised an assay which has been used to follow the reassembly of the unfractionated and fractionated (2BI and 2BII) cell wall glycoproteins. Reassembly has a pH optimum of 5, a temperature optimum of 20°C, and the final size of the reassembled fragments appears to be promoted by the minor component 2BI. Periodate oxidation experiments show that sugar residues, in particular mannose, are important for accurate reassembly. Using electron microscopy, the structure of the reassembled products has been elucidated, as have intermediate stages in the reassembly process.Abbreviations TRIS
Tris(hydroxymethyl)-methylamine
- SDS
Sodium dodecyl sulphate
- PAGE
Polyacrylamide gel electrophoresis
This is the fifth paper in a series entitled Structure composition and morphogenesis of the cell wall of Chlamydomonas reinhardii. The last paper in this series was Catt et al. (1976) |
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Keywords: | Cell wall Chlamydomonas Glyco-protein Hydroxyproline Self assembly |
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