Identification and characterization of the cAMP binding proteins of yeast by photoaffinity labeling

Charlotte Dery, Stephen Cooper, Michael A. Savageau, Sarah Scanlon

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Contrary to previous reports, we find the molecular weight of the major cAMP-binding protein in Saccharomyces cerevisiae to be 54,000 daltons. A number of lower molecular weight proteins have also been identified and are believed to be breakdown products of the major protein. The binding protein is soluble and specific for cyclic purine nucleotides with a 3′:5′ configuration.

Original languageEnglish (US)
Pages (from-to)933-939
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume90
Issue number3
DOIs
StatePublished - Oct 12 1979
Externally publishedYes

Fingerprint

Yeast
Labeling
Carrier Proteins
Yeasts
Molecular Weight
Molecular weight
Purine Nucleotides
Cyclic Nucleotides
Saccharomyces cerevisiae
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Identification and characterization of the cAMP binding proteins of yeast by photoaffinity labeling. / Dery, Charlotte; Cooper, Stephen; Savageau, Michael A.; Scanlon, Sarah.

In: Biochemical and Biophysical Research Communications, Vol. 90, No. 3, 12.10.1979, p. 933-939.

Research output: Contribution to journalArticle

Dery, Charlotte ; Cooper, Stephen ; Savageau, Michael A. ; Scanlon, Sarah. / Identification and characterization of the cAMP binding proteins of yeast by photoaffinity labeling. In: Biochemical and Biophysical Research Communications. 1979 ; Vol. 90, No. 3. pp. 933-939.
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