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Purification of Sulfhydryl Oxidase from Human Foreskin Tissue and Immunohistochemical Localization

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Authors
Park, Sang-Chul; Seo, Hye-Myung; Lee, Sang-Gyu; Kim, Woo-Ho; Song, Kye-yong; Eun, Hee-Chul
Issue Date
1992-12
Publisher
Seoul National University College of Medicine
Citation
Seoul J Med, Vol.33 No.4, pp. 239-246
Keywords
Sulfhydryl oxidaseHuman skinTissue 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
URI
http://hdl.handle.net/10371/6244
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College of Medicine/School of Medicine (의과대학/대학원)Dept. of Medicine (의학과)The Seoul Journal of MedicineThe Seoul Journal of Medicine Vol. 33 No.3 (1992)
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