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. 1985 Oct;50(4):951–957. doi: 10.1128/aem.50.4.951-957.1985

Identification of Glycolytic Enzyme Polypeptides on the Two-Dimensional Protein Map of Saccharomyces cerevisiae and Application to the Study of Some Wine Yeasts

Michel Brousse 1, Nelly Bataillé 1, Hélian Boucherie 1,*
PMCID: PMC291775  PMID: 16346922

Abstract

Using a modification of the basic two-dimensional polyacrylamide gel electrophoresis technique, the polypeptides of the protein map of Saccharomyces cerevisiae involved in glycolysis were investigated. This study resulted in a reassignment of two of the seven glycolytic enzyme polypeptides previously identified (Ludwig et al., Mol. Cell. Biol. 2:117-126, 1982), those corresponding to phosphoglycerate kinase and to alcohol dehydrogenase. It also resulted in the identification of two additional glycolytic polypeptides, the enolase B monomer and the glyceraldehyde phosphate dehydrogenase B monomer. The glycolytic enzymes polypeptides so identified were investigated in 5 laboratory strains (all S. cerevisiae) and in 11 commerical strains used for wine making (S. cerevisiae and Saccharomyces bayanus). It appeared highly significant that a particular electrophoretic variant of the glyceraldehyde phosphate dehydrogenase B monomer was found only in the wine yeasts. Furthermore, it was strongly suggested that S. cerevisiae and S. bayanus strains are distinguishible on the basis of a different electrophoretic migration of the enolase B monomer.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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