Related Experiment Videos
Studies on the Function of Disulfide Bond Cys(112)-Cys(115) in Arrowhead Proteinase Inhibitors
Zhi-Wei Xie1, Ming-Juan Luo, Cheng-Wu Chi
1State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry, Academia Sinica, Shanghai 200031, China.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao Acta Biochimica Et Biophysica Sinica
|January 1, 1996
Abstract:
Two cysteine residues which compose the disulfide bond Cys(112)-Cys(115) in the arrowhead inhibitor were replaced by Ala and Ser respectively, using site-directed mutagenesis. The mutant has similar inhibitory activities as that of the wild type. The result suggests that the disulfide bond of Cys(112)-Cys(115) in the arrowhead inhibitor is not indispensable to its inhibitory activity.