| Literature DB >> 1989578 |
Abstract
The domain structure of duck gizzard caldesmon was investigated. A single thiol group is located in the vicinity of the C-terminus of the protein. A simple method for the purification of a short (21 kDa) C-terminal peptide formed after chemical cleavage of caldesmon at cysteine residues was evolved. The C-terminal peptide of caldesmon interacts with calmodulin with an affinity one order of magnitude higher than that of native caldesmon. The Ca2+/phospholipid-dependent protein kinase (protein kinase C) transfers about 2 mol of phosphate per mol of caldesmon. All sites phosphorylated by protein kinase C are located in the short (21 kDa) C-terminal peptide of caldesmon. Phosphorylation does not affect the interaction of caldesmon with calmodulin.Entities:
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Year: 1991 PMID: 1989578 PMCID: PMC1149893 DOI: 10.1042/bj2730161
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857