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Purification of Sulfhydryl Oxidase from Human Foreskin Tissue and Immunohistochemical Localization
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- Authors
- Issue Date
- 1992-12
- Citation
- Seoul J Med, Vol.33 No.4, pp. 239-246
- Keywords
- Sulfhydryl oxidase ; Human skin ; Tissue distribution
- 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.
- ISSN
- 0582-6802
- Language
- English
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