The cell-wall glycoproteins of the green alga Scenedesmus obliquus. The predominant cell-wall polypeptide of Scenedesmus obliquus is related to the cell-wall glycoprotein gp3 of Chlamydomonas reinhardtii

Copyright © 2013 Elsevier Ireland Ltd. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant science : an international journal of experimental plant biology. - 1985. - 215-216(2014) vom: 28. Feb., Seite 39-47
1. Verfasser: Voigt, Jürgen (VerfasserIn)
Weitere Verfasser: Stolarczyk, Adam, Zych, Maria, Malec, Przemysław, Burczyk, Jan
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2014
Zugriff auf das übergeordnete Werk:Plant science : an international journal of experimental plant biology
Schlagworte:Journal Article Antibodies Cell wall Chlamydomonas reinhardtii Deglycosylation GP1 GP2 GP3 Glycoproteins Ig mehr... IgG PVDF Scenedesmus obliquus cell wall glycoprotein number 1 (Chlamydomonas reinhardtii) cell wall glycoprotein number 2 (Chlamydomonas reinhardtii) cell wall glycoprotein number 3 (Chlamydomonas reinhardtii) dGP100 dICW deglycosylated glycoprotein (final M(r) 100kDa) deglycosylated insoluble cell wall fraction immunoglobuline immunoglobuline class G polyvinylidene fluoride Cross-Linking Reagents Peptides
Beschreibung
Zusammenfassung:Copyright © 2013 Elsevier Ireland Ltd. All rights reserved.
The green alga Scenedesmus obliquus contains a multilayered cell wall, ultrastructurally similar to that of Chlamydomonas reinhardtii, although its proportion of hydroxyproline is considerably lower. Therefore, we have investigated the polypeptide composition of the insoluble and the chaotrope-soluble wall fractions of S. obliquus. The polypeptide pattern of the chaotrope-soluble wall fraction was strongly modified by chemical deglycosylation with anhydrous hydrogen fluoride (HF) in pyridine indicating that most of these polypeptides are glycosylated. Polypeptide constituents of the chaotrope-soluble cell-wall fraction with apparent molecular masses of 240, 270, 265, and 135 kDa cross-reacted with a polyclonal antibody raised against the 100 kDa deglycosylation product of the C. reinhardtii cell-wall glycoprotein GP3B. Chemical deglycosylation of the chaotrope-soluble wall fraction resulted in a 135 kDa major polypeptide and a 106 kDa minor component reacting with the same antibody. This antibody recognized specific peptide epitopes of GP3B. When the insoluble wall fraction of S. obliquus was treated with anhydrous HF/pyridine, three polypeptides with apparent molecular masses of 144, 135, and 65 kDa were solubilized, which also occured in the deglycosylated chaotrope-soluble wall fraction. These findings indicate that theses glycoproteins are cross-linked to the insoluble wall fraction via HF-sensitive bonds
Beschreibung:Date Completed 03.09.2014
Date Revised 30.09.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1873-2259
DOI:10.1016/j.plantsci.2013.10.011