Acid dnase acid phospho di esterase and acid phosphatase of new born rat epidermis skin multiple forms and glyco protein nature

Miyagawa, T.; Eguchi, Y.

Comparative Biochemistry and Physiology C Comparative Pharmacology 69(1): 39-44

1981


Accession: 004656036

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Abstract
Isoelectric focusing and concanavalin [Con]A-Sepharose were used to study multiple forms and glycoprotein nature of acid phosphohydrolases from newborn rat epidermis (skin). The crude extracts were focused in a 110 ml Ampholine gradient column with pH ranges of 3.5-10, 7-9 and 5-7. Acid DNase was resolved into 3 different forms, acid phosphodiesterase and acid phosphatase were separated into 2 different forms. All these enzymes separated by electrophoresis showed the optimal pH at 5.0. The bulk of acid DNase and acid phosphodiesterase were bound to the column of Con A-Sepharose, whereas about 30% of acid phosphatase passed through. About 50% of acid phosphatase were eluted with .alpha.-methyl-D-glucoside. About 22% of acid DNase and about 42% of acid phosphodiesterase were released from the column with .alpha.-methyl-D-glucoside. The glycoprotein nature of these acid hydrolases is indicated.