J. Walker, M. Walker
1960
Citations
0
Influential Citations
19
Citations
Journal
Archives of biochemistry and biophysics
Abstract
Abstract Papain, urease, and arginine-glycine transamidinase are strongly inhibited by formamidine disulfide. Evidence is presented which indicates that formamidine disulfide reacts with sulfhydryl groups of sensitive enzymes; presumably the initial reaction product is a mixed disulfide, analogous to the known mixed disulfide of cysteine and isothiourea. Formamidine disulfide reacts rapidly with enzyme sulfhydryl groups; the excess reagent decomposes within a few minutes at physiological pH. Utilizing these characteristics, evidence has been obtained which suggests that the essential sulfhydryl group of transamidinase is located at the active center of the enzyme.