Isolation and sequence analysis of a cDNA clone encoding the entire catalytic subunit of phosphorylase kinase |
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Authors: | E F da Cruz e Silva P T Cohen |
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Affiliation: | Department of Biochemistry, Medical Sciences Institute, University of Dundee, Dundee DD1 4HN, Scotland |
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Abstract: | Synthetic oligonucleotides have been used to isolate a 1.85 kb clone containing the full length coding sequence for the catalytic subunit of rabbit skeletal muscle phosphorylase kinase from a cDNA library constructed in lambda gt10. Sequence analysis of the clone predicted an amino acid sequence in agreement with a published primary structure. Inspection of the codon usage revealed a strong preference for G or C nucleotides at the third codon position as found for several other skeletal muscle proteins. This cDNA clone should facilitate identification of functional domains, including the calmodulin-binding site, and investigation of the molecular basis of X-linked phosphorylase kinase deficiencies. |
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