1887

Abstract

SUMMARY: Intra- and extracellular acid phosphatases were purified 88- and 65-fold respectively from photoheterotrophic Pringsheim. The purified enzymes differed in heat inactivation, substrate specificity, and inhibition by several divalent cations and NaF. Intracellular enzyme lost only 30 % of its activity by heating at 60 °C for 200 min whereas the extracellular enzyme lost 80 %. Both enzymes were active over a broad pH range from 2·2 to 5·2 and had an optimum pH of 4·8. Both had broad substrate specificity and differed in their relative ability to hydrolyse -glycerophosphate, phenolphthalein diphosphate, glucose-1 -phosphate, fructose-1,6-diphosphate, ADP and ATP. Both were inhibited by Co, Zn, Hg, Fe, arsenate, tartrate and fluoroacetate but differed in their inhibition by Cu, Hg and NaF. Intracellular acid phosphatase was more susceptible to inhibition by Hg and NaF, while extracellular acid phosphatase was more susceptible to inhibition by Cu. Chloromercuribenzoate and urea had no effect on either enzyme’s activity. EDTA stimulated the activity of both enzymes. The for the intra- and the extracellular enzymes was 0·5 and 0·33 m respectively with -nitrophenyl phosphate as the substrate.

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1974-07-01
2022-01-16
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