| Literature DB >> 3299375 |
K Takio, E A Kuenzel, K A Walsh, E G Krebs.
Abstract
The amino acid sequence of the 209-residue beta subunit of bovine lung casein kinase II has been determined. Excluding the amino-terminal blocking group, which was not identified, the molecular weight of the polypeptide chain is 24,239. A marked polarity of the beta subunit is indicated by clusters of negative charges in the amino-terminal region and of positive charges in the carboxyl-terminal region. Whereas the beta subunit shows no homology with any known protein, a segment of the sequence of the larger and microheterogeneous alpha subunit exhibits homology with the catalytic domains of other protein kinases, particularly with the yeast cell-division-control protein CDC28.Entities:
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Year: 1987 PMID: 3299375 PMCID: PMC305203 DOI: 10.1073/pnas.84.14.4851
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205