Acid deoxyribonuclease, acid phosphodiesterase and acid phosphatase of new born rat epidermis (skin): Multiple forms and glycoprotein nature

Abstract

1. Isoelectric focusing and concanavalin A-Sepharose were used to study multiple forms and glycoprotein nature of acid phosphohydrolases from new born rat epidermis (skin). 2. 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 three different forms, acid phosphodiesterase and acid phosphatase were separated into two different forms. All these enzymes separated by electrophoresis showed the optimal pH at 5.0. 3. The bulk of acid DNase and acid phosphodiesterase were bound to the column of concanavalin A-Sepharose, whereas about 30% of acid phosphatase passed through. About 50% of acid phosphatase were eluted with -methyl- d-glucoside. About 22% of acid DNase and about 42% of acid phosphodiesterase were released from the column with α-methyl- d-glucoside. These results indicate glycoprotein nature of these acid hydrolases.