Presence of multiple acid phosphatases activity in seedlings of cucumber, radish and rocket salad

Acid phosphatases (3.1.3.2) are a group of enzymes widely distributed in nature, which catalyze the hydrolysis of a variety of phosphate esters in the pH range of 4-6. We confirmed the presence of acid phosphatases in seedlings of cucumber (Cucumis sativus), radish (Raphanus sativus) and rocket salad (Eruca vesicaria) under different assay conditions using a rapid and simple preparation. The results showed that the optimum pH and temperature used for all species were close to 5.5 and 35°C, respectively. The enzyme was inhibited by molybdate, fluoride, azide, levamisole, orthovanadate, Zn2+ and Cu2+. Suramin had no effect on enzyme activity. The acid phosphatase from cucumber, radish and rocket salad hydrolyzed a wide variety of phosphate esters and the highest activity was observed with PPi, ATP and GTP. These results demonstrate that the enzyme investigated in this study is different from well known ester phosphate cleaving plant enzymes (apyrase and inorganic pyrophosphatases) and this preparation could be a useful tool to future toxicological studies and to study initially all isoforms of acid phosphatase.

Download Full-text

The route of non-enzymic and enzymic breakdown of 5-phosphoribosyl 1-pyrophosphate to ribose 1-phosphate

Biochemical Journal ◽

10.1042/bj2710621 ◽

1990 ◽

Vol 271 (3) ◽

pp. 621-625 ◽

Cited By ~ 8

Author(s):

H Trembacz ◽

M M Jezewska

Keyword(s):

Alkaline Phosphatase ◽

Aspergillus Niger ◽

Acid Phosphatases ◽

Cyclic Phosphate ◽

Ph Range ◽

Hydrolysis Of

Spontaneous decomposition of 5-phosphoribosyl 1-pyrophosphate at pH 5.5 was established to occur as follows: 5-Phosphoribosyl 1-pyrophosphate----5-phosphoribosyl 1,2-(cyclic)phosphate----ribose 1-phosphate----ribose Enzymic degradation of 5-phosphoribosyl 1-pyrophosphate by alkaline phosphatase from calf intestine and by acid phosphatases from potato and Aspergillus niger was found to proceed according to this pathway within the pH range 2.5-7.4 with accumulation of ribose 1-phosphate. In the case of alkaline phosphatase, Mg2+ ions inhibit the pyrophosphorolysis of 5-phosphoribosyl 1-pyrophosphate and stimulate the hydrolysis of ribose 1-phosphate.

Download Full-text

428. The acid phosphatase of mammary tissue of the cow and the rat

Journal of Dairy Research ◽

10.1017/s0022029900005859 ◽

1950 ◽

Vol 17 (3) ◽

pp. 306-311 ◽

Cited By ~ 1

Author(s):

J. E. C. Mullen

Keyword(s):

Alkaline Phosphatase ◽

Acid Phosphatase ◽

Replacement Therapy ◽

Marked Effect ◽

Mammary Tissue ◽

Optimum Ph ◽

Rate Of Hydrolysis ◽

Hydrolysis Of

1. Mammary tissue of the cow and the rat contains acid phosphatase. The respective pH optima are 5·5–5·8 and 6·0.2. The enzyme in cow mammary tissue is probably one of type AII in the Folley & Kay (10) classification.3. The acid phosphatase of cow mammary tissue is inhibited by a factor in raw cows' milk. This factor is destroyed by heat.4. On the basis of rate of hydrolysis of phenylphosphate at the optimum pH there is about 5 times more alkaline phosphatase in the mammary tissue of the cow than acid phosphatase.5. The effect of adrenalectomy and replacement therapy through the administration of cortical steroids has no marked effect on the acid phosphatase of rat mammary tissue.

Download Full-text

ACID PHOSPHATASE HYDROLYSIS OF PHOSPHORIC ESTERS

Canadian Journal of Biochemistry and Physiology ◽

10.1139/y55-067 ◽

1955 ◽

Vol 33 (1) ◽

pp. 539-544 ◽

Cited By ~ 1

Author(s):

G. E. Delory ◽

G. S. Wiberg ◽

Merle Hetherington

Keyword(s):

Acid Phosphatase ◽

Seminal Fluid ◽

Optimum Ph ◽

Rate Of Hydrolysis ◽

Hydrolysis Of

The rate of hydrolysis and optimum pH of hydrolysis of seminal fluid acid phosphatase have been studied for a number of phosphoric esters. As the acidity of the substrate increases there is a tendency for the rate of hydrolysis to increase and for the optimum pH to move farther away from neutrality. The increased rate of hydrolysis of phenol phosphates or of substituted phenol phosphates can not be accounted for by phenolase activity.

Download Full-text

The subcellular distribution of triphosphoinositide phosphomonoesterase in guinea-pig brain

Biochemical Journal ◽

10.1042/bj1280579 ◽

1972 ◽

Vol 128 (3) ◽

pp. 579-586 ◽

Cited By ~ 28

Author(s):

A. Sheltawy ◽

M. Brammer ◽

D. Borrill

Keyword(s):

Guinea Pig ◽

Subcellular Fractions ◽

Assay System ◽

Acid Phosphatases ◽

Alkaline Phosphatases ◽

Pig Brain ◽

Optimum Ph ◽

Ph Range ◽

Guinea Pig Brain ◽

Optimum Ph Range

1. Some properties of the triphosphoinositide phosphomonoesterase from the homogenates of guinea-pig brain were studied. The enzyme has an optimum pH range 6.7–7.3, is stimulated with KCl at a concentration of 0.1m, and under these conditions has Km1.43×10-4m. 2. A factor from the ‘pH5 supernatant’ of guinea-pig brain stimulates the enzyme activity over and above the stimulation produced by KCl. Subcellular fractions of guinea-pig brain varied in their response to the ‘pH5 supernatant’. Maximum stimulation was observed with the P1 fraction, containing myelin and nuclei. 3. An assay system for the enzyme was developed that contained optimum concentrations of both KCl and the ‘pH5 supernatant’. Acid phosphatases were inhibited by NaF, but, in contrast with previous work, no EDTA was added to the assay system to inhibit the alkaline phosphatases. This reagent inhibited the triphosphoinositide phosphomonoesterase. It was estimated that the remaining fraction of non-specific phosphatases can account for only 14% of the observed triphosphoinositide phosphomonoesterase activity. 4. Subcellular fractions of guinea-pig brain were characterized by electron microscopy and subcellular markers. The triphosphoinositide phosphomonoesterase exhibited a distribution between the fractions similar to that of 5′-nucleotidase, but different from that of alkaline phosphatase.

Download Full-text

Comparison of the Thermostability Properties of Three Acid Phosphatases from Molds: Aspergillus fumigatusPhytase, A. niger Phytase, and A. nigerpH 2.5 Acid Phosphatase

Applied and Environmental Microbiology ◽

10.1128/aem.64.11.4446-4451.1998 ◽

1998 ◽

Vol 64 (11) ◽

pp. 4446-4451 ◽

Cited By ~ 93

Author(s):

Markus Wyss ◽

Luis Pasamontes ◽

Roland Rémy ◽

Josiane Kohler ◽

Eric Kusznir ◽

...

Keyword(s):

Acid Phosphatase ◽

Aspergillus Niger ◽

Enzymatic Activity ◽

Conformational Changes ◽

Animal Feed ◽

Heat Denaturation ◽

Acid Phosphatases ◽

Active Conformation ◽

Feed Supplements ◽

Optimum Ph

ABSTRACT Enzymes that are used as animal feed supplements should be able to withstand temperatures of 60 to 90°C, which may be reached during the feed pelleting process. The thermostability properties of three histidine acid phosphatases, Aspergillus fumigatus phytase,Aspergillus niger phytase, and A. niger optimum pH 2.5 acid phosphatase, were investigated by measuring circular dichroism, fluorescence, and enzymatic activity. The phytases ofA. fumigatus and A. niger were both denatured at temperatures between 50 and 70°C. After heat denaturation at temperatures up to 90°C, A. fumigatus phytase refolded completely into a nativelike, fully active conformation, while in the case of A. niger phytase exposure to 55 to 90°C was associated with an irreversible conformational change and with losses in enzymatic activity of 70 to 80%. In contrast to these two phytases,A. niger pH 2.5 acid phosphatase displayed considerably higher thermostability; denaturation, conformational changes, and irreversible inactivation were observed only at temperatures of ≥80°C. In feed pelleting experiments performed at 75°C, the recoveries of the enzymatic activities of the three acid phosphatases were similar (63 to 73%). At 85°C, however, the recovery of enzymatic activity was considerably higher for A. fumigatusphytase (51%) than for A. niger phytase (31%) or pH 2.5 acid phosphatase (14%). These findings confirm that A. niger pH 2.5 acid phosphatase is irreversibly inactivated at temperatures above 80°C and that the capacity of A. fumigatus phytase to refold properly after heat denaturation may favorably affect its pelleting stability.

Download Full-text

Biochemical and histochemical studies of alkaline and acid phosphatases in a digenetic trematode,Pegosomum egretti

Journal of Helminthology ◽

10.1017/s0022149x00008518 ◽

1986 ◽

Vol 60 (4) ◽

pp. 293-298 ◽

Cited By ~ 1

Author(s):

Indra Rajvanshi ◽

K. L. Mali

Keyword(s):

Alkaline Phosphatase ◽

Enzyme Activity ◽

Acid Phosphatase ◽

Raw Materials ◽

Digenetic Trematode ◽

Acid Phosphatases ◽

Alkaline Phosphatases ◽

Optimum Ph ◽

Standard Techniques ◽

Alkaline And Acid Phosphatases

ABSTRACTThe biochemistry and histochemistry ofPegosomum egrettihave been studied using standard techniques. Phosphatases were analysed colorimetrically; the optimum pH for acid phosphatase activity was 5·0 and for alkaline phosphatase was 10·0. The results were compared with those of other trematodes. Histochemical localization of acid and alkaline phosphatases revealed differences in enzyme activity in various tissues. These differences in the site and pattern of distribution of the two enzymes have been discussed in relation to transport of raw materials and the metabolism of the cell concerned.

Download Full-text

Acid phosphatases and ribonucleases from Dactylis glomerata seeds. I. Chromatographic and electrophoretic heterogeneity of the enzymes

Acta Societatis Botanicorum Poloniae ◽

10.5586/asbp.1978.040 ◽

2015 ◽

Vol 47 (4) ◽

pp. 441-453 ◽

Cited By ~ 1

Author(s):

Eleonora Wieczorek ◽

Janina Wiśniewska ◽

Bronisława Morawiecka

Keyword(s):

Acid Phosphatase ◽

Sodium Acetate ◽

Specific Activity ◽

Deae Cellulose ◽

Dactylis Glomerata ◽

Molecular Forms ◽

Acid Phosphatases ◽

Sodium Acetate Buffer ◽

Optimal Activity ◽

Optimum Ph

Acid phosphatase and ribonuclease extracted with 0.1 M sodium acetate buffer, pH 5.1 from Dactylis glomerata seeds, and partially purified by means of 70% ethanol precipitation showed electrophoretic and Chromatographic heterogeneity. After chromatography on DEAE-cellulose acid phosphatase and ribonuclease were separated into four peaks. Nonadsorbing acid phosphatase on DEAE-cellulose (peak I) was separated into four peaks on CM-cellulose. The highest activity (11 units/mg) was found in fraction b (acid phosphatase Ib). The enzyme was activated by Mg2+, Ca2+, Li+, Cs+, K+ ions and inhibited by Cu2+, Zu2+, F- and Mo-6 at optimum pH 5.0. Strong absorbing ribonuclease on DEAE-cellulose (peak IV) was further separated on G-200 Sephadex into two molecular forms: RN-asa1 and RN-ase2. Ribonuclease l, a thermolabile enzyme with specific activity 807 units/mg, showed an optimal activity at pH 4.8-5.1.

Download Full-text

Phosphatase activity of Poa pratensis seeds. III. Effect of fluoride, citrate, urea and other substances on the activity of acid phosphatase Ia2 and Ia3

Acta Societatis Botanicorum Poloniae ◽

10.5586/asbp.1978.007 ◽

2015 ◽

Vol 47 (1–2) ◽

pp. 83-89

Author(s):

Irena Lorenc-Kubis ◽

Bronisław Morawiecka

Keyword(s):

Acid Phosphatase ◽

Phosphatase Activity ◽

Mixed Type ◽

Poa Pratensis ◽

Acid Phosphatases ◽

Other Substances ◽

Inhibited Acid ◽

Hydrolysis Of

Effects of fluoride, citrate, urea and other substances on the activity of acid phosphatase a2 and a3 toward p-nitrophenylphosphate and phenylphosphate were investigated. Both enzymes were inhibited by fluoride, p-chloromercuribenzoate and oxalate. Fluoride inhibited acid phosphatase a2 noncorapetitively with p-mitrophenylphosphate, whereas acid phosphatase a3 showed inhibition of mixed type. Hydrolysis of phenylphosphate by both acid phosphatases was activated by citrate. Cytosine and uridine inhibited the activity of phosphatase a2 toward p-nitrophenylphosphate and phenylphosphate, but no effect was observed in case of acid phosphatase a3. After 30 min. incubation with 4 M urea both enzymes lost about 30% of activity.

Download Full-text

ADENYLATE AND 2,6-DIAMINOPURINE RIBONUCLEOTIDE PYROPHOSPHORYLASE ACTIVITIES OF L CELLS

Canadian Journal of Biochemistry ◽

10.1139/o67-052 ◽

1967 ◽

Vol 45 (4) ◽

pp. 435-449 ◽

Cited By ~ 6

Author(s):

D. G. R. Blair

Keyword(s):

Radioactive Tracer ◽

Mouse Fibroblast ◽

Enzyme Inactivation ◽

Cell Extracts ◽

Zero Order Kinetics ◽

Tracer Techniques ◽

Optimum Ph ◽

Ph Range ◽

Kinetics Of ◽

Assay Conditions

The reaction kinetics of adenylate (AMP) and 2,6-diaminopurine ribonucleoside 5′-monophosphate (DAPRP) pyrophosphorylase activities of extracts of L-strain mouse fibroblast cells were studied by chromatographic and radioactive tracer techniques. The apparent Kmvalues found for 5-phosphoribosyl-α-1-pyrophosphate (PRPP) were 6.9 × 10−5 M for AMP pyrophosphorylase activity and 3.6 × 10−4 M for DAPRP pyrophosphorylase activity. The apparent Kmfound for adenine was 3.0 × 10−5 M, whereas the apparent Kmcalculated for 2,6-diaminopurine was 1.8 × 10−3 M. An optimum pH of 7.6 was found for AMP pyrophosphorylase, whereas an optimum pH range of 7.6–7.9 was found for DAPRP pyrophosphorylase activity. Under assay conditions of zero-order kinetics, the AMP pyrophosphorylase activities of L-cell extracts were approximately twice the DAPRP pyrophosphorylase activities of the same extracts.AMP and DAPRP were found to be the major products of the AMP and DAPRP pyrophosphorylase reactions, respectively. DAPRP was analyzed chemically and spectrophotometrically, and absorption spectra at different pH values are presented.The effects of sulfate ions, storage, and enzyme inactivation techniques on enzyme activities were also studied.

Download Full-text

Phosphorus metabolism in the coral–zooxanthellae symbiosis: characterization and possible roles of two acid phosphatases in the algal symbiont Symbiodinium sp

Proceedings of the Royal Society of London Series B Biological Sciences ◽

10.1098/rspb.1989.0076 ◽

1989 ◽

Vol 238 (1291) ◽

pp. 193-202 ◽

Cited By ~ 16

Keyword(s):

Inorganic Phosphate ◽

Physiological Role ◽

Phosphate Esters ◽

Phosphorus Metabolism ◽

Acid Phosphatases ◽

Hard Coral ◽

Algal Symbiont ◽

Acropora Formosa ◽

Hydrolysis Of

Cell-free extracts of zooxanthellae ( Symbiodinium sp.) from the hard coral Acropora formosa contained two acid phosphatases that were resolved by affinity chromatography on concanavalin-A-Sepharose. The enzymes had similar properties, with the exception that phosphatase P-1 hydrolysed polyphosphate and pyrophosphate, whereas phosphatase P-2 had no activity towards either. The high activity of phosphatase P-1 with polyphosphate implies that the physiological role of this enzyme may be the mobilization of this phosphate storage compound. The physiological substrate of phosphatase P-2 is unknown, but the most likely role of this enzyme is the hydrolysis of phosphate esters exterior to the plasmalemma, before uptake of the released inorganic phosphate by the algal transport system. Cultured zooxanthellae ( S. kawagutii ) contained phosphatase P-2 only; the significance of this difference is unknown. The activities of P-1 and P-2 were always high in freshly isolated zooxanthellae, and both activities were repressed after incubation in phosphate-supplemented media. The implication is therefore that the algae in the coral-zooxanthellae symbiosis may be phosphate limited.

Download Full-text