title: Some properties of duck gizzard caldesmon.
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.
authors.affiliation: Department of Biochemistry, School of Biology, Moscow State University, U.S.S.R.
authors.forename: A V
authors.initials: AV
authors.lastname: Vorotnikov
authors.forename: N B
authors.initials: NB
authors.lastname: Gusev
mesh_terms: D000818:Animals; D002118:Calcium / Q000378:metabolism; D002148:Calmodulin-Binding Proteins / Q000737:chemistry*; D004372:Ducks; D004591:Electrophoresis, Polyacrylamide Gel; D005895:Gizzard, Avian / Q000737:chemistry*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013438:Sulfhydryl Compounds
chemical_list: D002148:Calmodulin-Binding Proteins; D013438:Sulfhydryl Compounds; D011493:Protein Kinase C; D002118:Calcium