U. Wojda et J. Kuznicki, CHARACTERIZATION OF CALCYCLIN FRAGMENTS OBTAINED BY CNBR-CLEAVAGE, International Journal of Biochemistry, 25(7), 1993, pp. 999-1007
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.