Purification of Sulfhydryl Oxidase from Human Foreskin Tissue and Immunohistochemical Localization

Abstract

Human sulfhydryl oxidase, catalyzing the conversion of either free or bound thiol to disulfide compound, was isolated from human skin tissue to apparent homogeneity through multiple steps of ammonium sulfate salting-out, DEAE-cellulose chromatography, CM-cellulose chromatography and ACA54 gel filtration. The enzyme was shown to have a molecular weight of 65 kDa and a specific activity of 8.39 x 103 Ufmg protein. The specific polyclonal antibody was raised, with which the tissue distribution of the enzyme was studied immunohistochemically. The enzyme is present ubiquitously in most human tissues. However, the granular layer of the epidermis, stromal tissues of the breast and uterine cervix, hepatocytes and islets of the pancreas are noted to contain a comparatively high amount of the enzyme.