Purification, characterization and partial amino acid sequence of glycogen synthase from Saccharomyces cerevisiae

A. Carabaza, J. Arino, J. W. Fox, C. Villar-Palasi, J. J. Guinovart

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4 Citations (Scopus)

Abstract

Glycogen synthase from Saccharomyces cerevisiae was purified to homogeneity. The enzyme showed a subunit molecular mass of 80 kDa. The holoenzyme appears to be a tetramer. Antibodies developed against purified yeast glycogen synthase inactivated the enzyme in yeast extracts and allowed the detection of the protein in Western blots. Amino acid analysis showed that the enzyme is very rich in glutamate and/or glutamine residues. The N-terminal sequence (11 amino acid residues) was determined. In addition, selected tryptic-digest peptides were purified by reverse-phase h.p.l.c. and submitted to gas-phase sequencing. Up to eight sequences (79 amino acid residues) could be aligned with the human muscle enzyme sequence. Levels of identity range between 37 and 100%, indicating that, although human and yeast glycogen synthases probably share some conversed regions, significant differences in their primary structure should be expected.
Original languageEnglish
Pages (from-to)401-407
JournalBiochemical Journal
Volume268
Issue number2
DOIs
Publication statusPublished - 1 Jan 1990

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