PMID: 2492822Feb 6, 1989Paper

Beta-glucosidase activity in porcine epidermis

Biochimica Et Biophysica Acta
P W Wertz, D T Downing

Abstract

One of the final steps in epidermal differentiation is the conversion of glucosylceramides to ceramides, which presumably is mediated by a beta-glucosidase activity. In the present manuscript, it is demonstrated that pig epidermis contains beta-glucosidase activity which is 3.3-times greater than alpha-glucosidase and 5-times greater than beta-galactosidase. This beta-glucosidase was found to be maximally active between pH 3.0 and essentially inactive at pH 9.0. In a standard assay, a disk of epidermis (8 mg dry weight) was submerged in 1 ml of 50 mM acetate buffer (pH 4.7) containing 150 mM NaCl and 15 mM p-nitrophenyl-beta-D-glucopyranoside at room temperature. Reaction was stopped by addition of 4 ml of 100 mM (pH 9.0) borate buffer and the supernatant was transferred to a separate tube. The nitrophenylate anion was then measured spectrophotometrically at a wavelength of 405 nm. Under these conditions, product formation was linear for at least 90 min and an apparent Km of 244 microM was estimated for the synthetic substrate. When the amount of epidermis in the assay was varied, the formation of product per unit of time remained proportional to the amount of epidermis. The level of beta-glucosidase activity was enhanced sligh...Continue Reading

References

Jul 1, 1975·The British Journal of Dermatology·P D Mier, J J van den Hurk
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Jan 1, 1981·Methods in Enzymology·E Heymann, R Mentlein

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Citations

Sep 12, 2006·FEBS Letters·Walter M HolleranYoshikazu Uchida
Apr 1, 1992·International Journal of Cosmetic Science·J P Forestier
Sep 20, 2005·The Journal of Experimental Biology·Agustí Muñoz-Garcia, Joseph B Williams
Apr 16, 1998·The Journal of Investigative Dermatology·N L MarchellW M Holleran
Jun 1, 1993·Comparative Biochemistry and Physiology. Comparative Physiology·F ChangC A Squier

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