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J. Biochem, 1984, Vol. 96, No. 4 1175-1182
© 1984 Japanese Biochemical Society

research-article

Calcium Binding to Tryptic Fragments of Calmodulin1

Osamu MINOWA and Koichi YAGI

Department of Chemistry, Faculty of Science, Hokkaido University Kita-ku, Sapporo, Hokkaido 060

Fragments of scallop testis calmodulin were prepared by tryptic digestion. One peptide consisted of 75 amino acid residues from N-acetylalanine to lysine at position 75 (F12) and the other of 71 residues from aspartic acid at position 78 to C-terminal lysine (F34). Flow dialysis and equilibrium dialysis experiments revealed the existance of two Ca2+ binding sites in each fragment. Half-saturating concentrations of the Ca2+ titration curves were 11 µM for F12 and 3.2 µM for F34, and Hill coefficients were obtained as 1.14 and 1.84, respectively. The results indicate that the high-affinity sites for Ca2+ are located on the C-terminal region of the calmodulin.

The sum of the two Ca2+ titration curves of F12 and F34 fits well to the curves of Ca2+ binding to intact calmodulin. This shows that the characteristic of Ca2+ bindings in intact calmodulin did not change after separation of the whole molecule into two domains, F12 and F34. The domains corresponding to F12 and F34 may exist independently from each other in the intact calmodulin molecule.

1This study was supported in part by a Grant-in-Aid from the Muscular Dystrophy Association of America, Inc.


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