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July 1955

Histochemical Studies of Skin: Localization of Dehydrogenase Activity. Protein-Bound Sulfhydryl and Disulfide Groups

Author Affiliations

Jacksonville, Fla.; Birmingham, Ala.

From the Pathology Laboratory (Dr. Foraker, Pathologist), Baptist Memorial Hospital, and the Department of Biochemistry (Dr. Wingo, Associate Professor), University of Alabama Medical College and School of Dentistry.

AMA Arch Derm. 1955;72(1):1-6. doi:10.1001/archderm.1955.03730310003001

Succinic dehydrogenase activity, proteinbound sulfhydryl and disulfide groups, all having relationship to growth, metabolism, or maturation of epidermal cells, were studied in 102 specimens of human skin.

Succinic dehydrogenase plays a vital role in the respiratory processes of most living cells and forms a link in the chain of reactions concerned with the oxidation of lipids, carbohydrates, and proteins.1 Sites of succinic dehydrogenase activity have been found to correlate with regions of cell growth in various contexts. In the uterine cervix manifestation of this enzyme activity occurs in the basal layer of normally maturing portio vaginalis epithelium, but is found more diffusely through metaplastic epithelium and in squamous-cell carcinoma.2

Protein-bound sulfhydryl groups are essential for the activity of many enzymes.3 They serve as protein links and are important in varied cell functions. Sulfhydryl groups have an important function in

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