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J. Biochem, 1986, Vol. 99, No. 5 1409-1416
© 1986 Japanese Biochemical Society

research-article

Limited Digestion of Cahnodulin with Trypsin in the Presence or Absence of Various Metal Ions

Hirsohi KAWASAKI1, Yasuyuki KUROSU2, Hisataka KASAI, Toshiaki ISOBE and Tsuneo OKUYAMA

Department of Chemistry, Faculty of Science, Tokyo Metropolitan University 2-1-1, Fukasawa, Setagaya-ku, Tokyo 158

The limited proteolysis of bovine brain calmodulin with trypsin in the presence or absence of various metal ions was reinvestigated in detail by HPLC. With metal ion-free calmodulin, limited proteolysis occurred at Arg 37 and Arg 106 with a cleavage ratio of 1 to 5, resulting in fragments consisting of residues 1–37, 38–148, 1–106 and 107–148. Fragments 1–37 and 107–148 accumulated under metal ionfree conditions. In the presence of calcium ions, the susceptibility of these sites to trypsin decreased and limited proteolysis occurred at Lys 77 as already reported by other workers. Fragment 78-148 accumulated, whereas fragment 1–77 was un stable under calcium-bound conditions, giving smaller peptides. Upon binding of manganese ions, calmodulin underwent a change of susceptibility to trypsin, resulting in cleavage at Lys 77, as observed for calcium-bound calmodulin. In the presence of zinc or magnesium ions, calmodulin was cleaved at the same sites as metal ion-free calmodulin under conditions where calmodulin would be expected to bind the respective ions.

1 Present address: The Tokyo Metropolitan Institute of Medical Science, 3–18, Honkomagome, Bunkyo-ku, Tokyo 113.

2 Present address: Japan Spectroscopic Co., Ltd., Hachiohji, Tokyo 192.


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