Characterization of calcyclin fragments obtained by CNBr-cleavage.
1. Two calcyclin fragments were obtained by CNBr-cleavage. 2. One fragment represented N-terminal end of a molecule (residues 1-56), and another one a C-terminal end (residues 57-89). 3. Properties of intact calcyclin such as binding of calcium, binding to hydrophobic resins and interaction with calcyclin specific antibodies were not retained by these fragments. 4. However, both fragments were able to form dimers and higher forms of aggregates as seen for uncleaved calcyclin. 5. This indicates that both halves of the molecule contain the regions responsible for non-covalent interaction which might participate in dimer formation.
Wojda
U
U
Nencki Institute of Experimental Biology, Warszawa, Poland.
Kuźnicki
J
J
D000595:Amino Acid Sequence; D000818:Animals; D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D002286:Carcinoma, Ehrlich Tumor; D002417:Cattle; D003488:Cyanogen Bromide / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D009418:S100 Proteins; D013050:Spectrometry, Fluorescence; D014407:Tumor Cells, Cultured
D002135:Calcium-Binding Proteins; D009418:S100 Proteins; D003488:Cyanogen Bromide; D002118:Calcium