Studies on the Function of Disulfide Bond Cys(112)-Cys(115) in Arrowhead Proteinase Inhibitors.
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.
Xie
Zhi-Wei
ZW
State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry, Academia Sinica, Shanghai 200031, China.
Luo
Ming-Juan
MJ
Chi
Cheng-Wu
CW