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J. Biochem, 1978, Vol. 83, No. 3 747-753
© 1978 Japanese Biochemical Society

research-article

Studies on Soybean Trypsin Inhibitors

XIII. Preparation and Characterization of Active Fragments from Bowman-Birk Proteinase Inhibitor1

Shoji ODANI and Tokuji IKENAKA

Department of Biochemistry, Niigata University School of Medicine Niigata, Niigata 951

Soybean Bowman-Birk inhibitor, a double-headed inhibitor of trypsin and {alpha}-chymotrypsin, was treated with cyanogen bromide and then pepsin to yield two inhibitory active fragments. Structural investigation showed that one of the fragments was derived from the trypsin inhibitory domain and the other from the chymotrypsin inhibitory domain of the inhibitor.

In contrast to the unusual stability of the native inhibitor, the separated domains were less stable and could be inactivated with excess proteinases. These results suggest that the legume double-headed inhibitors acquired their unusual stability by duplicating an ancestral single-headed structure.

1 This study was supported in part by a grant from the Ministry of Education, Science and Culture of Japan. A preliminary account of this work has appeared (l).


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