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ACID HYDROLASES IN THE HUMAN EPIDERMIS
40
Citations
17
References
1972
Year
Skin DevelopmentAcid PhosphataseBiochemistryCellular EnzymologyNatural SciencesCutaneous BiologyBioanalysisGlycobiologyHuman EpidermisGlycosylationWound HealingDermatologyCellular BiochemistryMetabolismMedicineDermal StructureProtein PhosphorylationNormal Human Epidermis
α‐ and β‐D‐glucosidases, β‐D‐glucuronidase, α‐ and β‐D‐mannosidases, α‐and β‐D‐glucosidases, β‐D‐fucosidase, α‐L‐fucosidase and β‐D‐Nacetyglucosaminidase activities were measured in the human epidermis using p‐nitrophenol and 4‐methylumbelliferone compounds as substrates. There was no appreciable difference in activities noted when both substrates were compared. Acid phosphatase was assayed with p‐nitrophenol phosphate and α‐naphthyl acid phosphate as substrates. Acid phosphatase seemed to be present, both free in the cytoplasm and in lysosomes. These 2 activities could not be differentiated by agarose electrophoresis (both fractions showed 2 anodally migrating bands). Some of the biochemical properties of these acid hydrolases from the normal human epidermis are presented.
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