CHARACTERIZATION OF CALCYCLIN FRAGMENTS OBTAINED BY CNBR-CLEAVAGE

1. Two calcyclin fragments were obtained by CNBr-cleavage. 2. One frag ment represented N-terminal end of a molecule (residues 1-56), and ano ther one a C-terminal end (residues 57-89). 3. Properties of intact ca lcyclin such as binding of calcium, binding to hydrophobic resins and interaction with calcyclin specific antibodies were not retained by th ese fragments. 4. However, both fragments were able to form dimers and higher forms of aggregates as seen for uncleaved calcyclin. 5. This i ndicates that both halves of the molecule contain the regions responsi ble for non-covalent interaction which might participate in dimer form ation.