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

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

doi:10.1016/0006-291X(79)91917-X

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 journal › Article

9 Scopus citations

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 language	English (US)
Pages (from-to)	933-939
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	90
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(79)91917-X
State	Published - Oct 12 1979
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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Dery, C., Cooper, S., Savageau, M. A., & Scanlon, S. (1979). Identification and characterization of the cAMP binding proteins of yeast by photoaffinity labeling. Biochemical and Biophysical Research Communications, 90(3), 933-939. https://doi.org/10.1016/0006-291X(79)91917-X

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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.",

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AB - 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.

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