Identification of a Novel Hepatic Calcium-Binding Protein

摘要: Summary Calcium binding activity in the 100,000 × g supernatant of bovine liver has been isolated by a procedure involving DEAE cellulose and Sephadex G-100 chromatography. In addition to calmodulin, two new high affinity calcium proteins have identified. On gel filtration chromatography these migrate with apparent molecular weights 83,700 51,400; whereas sodium dodecyl sulfate polyacrylamide electrophoresis, identically Mr 63,000. presence millimolar Mg2+, both bind up one mol Ca2+/mol protein. Half-maximal occurs at approximately 0.1 M Ca2+. Amino acid compositional analysis reveals that are acidic, contain about 40% glx asx. Peptide mapping procedures suggest may be highly homologous or multiple forms single The results show existence protein(s) other than calmodulin hepatic cytosol.