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Analysis of Leaf Proteins by Two-Dimensional Gel Electrophoresis
Author(s) -
Catherine Colas des FrancsSmall,
Hervé Thiellement,
Dominique de Vienne
Publication year - 1985
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.78.1.178
Subject(s) - gel electrophoresis , sodium dodecyl sulfate , protein subunit , ribulose 1,5 bisphosphate , chemistry , biochemistry , degradation (telecommunications) , pyruvate carboxylase , electrophoresis , chromatography , two dimensional gel electrophoresis , rubisco , extraction (chemistry) , polyacrylamide gel electrophoresis , enzyme , gene , proteomics , telecommunications , computer science
A previous genetic analysis by two-dimensional electrophoresis of wheat leaf proteins led us to hypothesize that several polypeptides were degradation products of the large subunit of ribulose bisphosphate carboxylase/oxygenase (EC 4.1.1.39).VARIOUS EXTRACTION PROCEDURES INCLUDING THE USE OF PROTEINASE INHIBITORS ALLOWED US TO: (a) confirm that the suspected polypeptides are indeed degradation products; (b) find out under which conditions the proteinases act; (c) find a method which prevents degradation, by boiling the extract in the presence of sodium dodecyl sulfate and 2-mercaptoethanol.

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