Purification and characterization of guinea-pig epidermal acid phosphatase

The British Journal of Dermatology
T MiyagawaH Urabe

Abstract

Guinea-pig epidermal acid phosphatase has been purified approximately 120-fold by a procedure including acid treatment, CM-cellulose and DEAE-cellulose chromatography, and gel filtration on Sephadex G-100. The enzyme had a pH optimum at 5-0 and the optimal temperature for activity was approximately 50 degrees C. The enzyme was not activated by divalent cations or 2-mercaptoethanol, but it was inhibited by p-chloromercuribenzoate and by fluoride. The km value for p-nitrophenyl phosphate was 1-31x10-4 M, the molecular weight was about 73,000 as determined by Sephadex G-100 gel filtration and the isoelectric point was 6.1. The enzyme hydrolyzed deoxyribonucleoside monophosphates to deoxyribonucleosides.

References

Nov 14, 1975·Archives of Dermatological Research·T MiyagawaH Urabe
Dec 1, 1974·The Journal of Investigative Dermatology·T MiyagawaH Urabe
Jan 1, 1968·Archives of Biochemistry and Biophysics·M H RagabA L Tappel
Aug 1, 1962·The Journal of Investigative Dermatology·C HODGSON

Related Concepts

Acid Phosphatase
Metazoa
Cations, Divalent
Deoxyribonucleotides
Cavia porcellus
Hydrogen-Ion Concentration
Isoelectric Point
Protein Denaturation
Skin

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