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