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Recent studies on the structure and function of the tartrate-resistant acid phosphatase (Mr 38 000) of the frog liver arc reviewed. The nature of the enzyme heterogeneity is elucidated on a molecular and physiologi­cal basis. The following structure-activity relationship is proposed: the enzyme protein is modified by glycosylation processes leading to forma­tion of the different enzyme forms. The oligosaccharide chain stabilizes the final structure of the enzyme forms with altered conformation causing different exposure of the essential functional groups (e.g. sulfliydryl residues, antigen determinants). This leads to different physiological events necessary for fulfillment of metabolic requirements of the cell.
Acid phosphatase (AcP) is a commonly observed enzyme in animal semen. In this study, AcP in rainbow trout (Oncorhynchus mykiss) spermatozoa was partly purified and characterized. Extraction in 0.85% NaCl with 0.1% Triton X-100 enabled obtaining 95% of total AcP activity observed in sperm supernatant. Kinetic characteristics were described for the enzyme from sperm extract and for the partly purified enzyme following gel filtration. The optimum pH was 5.8 for unpurified and 5.6 for partly purified enzyme. The affinity of the substrates measured in the sperm extract for p-nitrophenylphosphate dissodium salt and b-glycerophosphate was Km = 1.5 × 10-3M and Km = 1.9 × 10-3M, respectively. The Km for partly purified enzyme was similar at 1.67 × 10-3M measured with p-nitrophenylphosphate dissodium salt. L-tartaric acid and ammonium molybdate were the inhibitors of AcP for unpurified and partly purified enzyme. SDS-PAGE electrophoresis revealed that AcP from rainbow trout had a molecular weight of about 41 kDa.
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Remediation of soil contaminated with cadmium

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The search for the best solutions to restore soil balance is essential for attaining a stable and sustainable agricultural development worldwide. This research, which makes a contribution to these investigations, focuses on four substances (two innovative ones: basalt flour, brown algal extract, and two classic soil improvers: finely ground barley straw and compost) which can potentially alleviate the inhibitory effect of Cd2+ on the soil environment. The following were analyzed: the activity of acid phosphatase and alkaline phosphatase, counts of Pseudomonas sp., cellulolytic bacteria, copiotrophic bacteria and copiotrophic spore-forming bacteria, and the yield of spring barley. Cadmium (Cd2+) was applied as CdCl2 · 2.5H2O in the following doses: 0, 4, 40, 80, 120, 160, and 200 mg Cd2+ kg-1 of soil. For a more complete assessment of the soil, its biochemical properties and the counts of microorganisms were scrutinized with the following indices: RS – soil resistance, R:S – rhizosphere effect and EF – fertilization effect of the contamination alleviating substances. It was found that alkaline phosphatase is more sensitive to cadmium contamination of the soil than acid phosphatase. Cadmium did not exert any inhibitory effect on the number of microorganisms present or the yield of spring barley. Cellulolytic bacteria were the least sensitive to stress associated with the accumulation of high cadmium doses in the soil, whereas copiotrophic bacteria were the most sensitive microorganisms to the above stressor. The ability of cadmium-polluted soil to restore homeostasis depended on the type of a soil improver and the level of soil contamination. Negative consequences of cadmium pollution were effectively mitigated by straw, but less so by brown algal extract and basalt flour.
The properties of plant purple acid phosphatases (PAPs), metallophosphoesterases present in some bacteria, plants and animals are reviewed. All members of this group contain a characteristic set of seven amino-acid residues involved in metal li- gation. Animal PAPs contain a binuclear metallic center composed of two irons, whereas in plant PAPs one iron ion is joined by zinc or manganese ion. Among plant PAPs two groups can be distinguished: small PAPs, monomeric proteins with molecular mass around 35 kDa, structurally close to mammalian PAPs, and large PAPs, homodimeric proteins with a single polypeptide of about 55 kDa. Large plant PAPs exhibit two types of structural organization. One type comprises enzymes with subunits bound by a disulfide bridge formed by cysteines located in the C-terminal region around position 350. In the second type no cysteines are located in this posi­tion and no disulfide bridges are formed between subunits. Differences in structural organisation are reflected in substrate preferences. Recent data reveal in plants the occurrence of metallophosphoesterases structurally different from small or large PAPs but with metal-ligating sequences characteristic for PAPs and expressing pro­nounced specificity towards phytate or diphosphate nucleosides and inorganic pyrophosphate.
Frog liver acid phosphatase hydrolyzes phosphotyrosine at acidic pH optimum. Mn2+, Ca2+ and Mg2+ (but not Zn2+) ions modulate this activity by shifting its pH optimum to physiological pH. This effect is not observed when p-nitrophenylphos-phate is used as a substrate. Phosphoserine and phosphothreonine are not hydrolyzed under the same conditions.
The aim of the study has been to determine the effect of soil contamination with zinc on the activity of soil enzymes. The study consisted of two laboratory experiments. Same, light loamy soil of pH 7.1, was used in both experiments. The variables in the first experiment were: a degree of soil contamination with zinc in mg Zn kg-1 d.m. of soil: 0, 5, 500, 1000, 1500 and 2000; dose of cellulose in g kg-1 d.m. of soil: 0, 15, and time of soil incubation (15 – 120 days). In the second experiment the following variables were tested: the degree of soil contamination with zinc in mg Zn kg-1 d.m. of soil: 0, 1000 and 2000; soil pH: 7.1, 6.4 and 5.5, and the time of soil incubation (15 – 120 days). The results of the experiments demonstrated that contamination of soil with zinc led to depressed activity of dehydrogenases, urease, acid phosphatase and alkaline phosphatase. Dehydrogenases and urease appeared to be more vulnerable to zinc contamination than phosphatases. The soil enzymes were adversely affected not only by zinc contamination but also by increasing soil acidity. According to their vulnerability to soil acidity the soil enzymes can be ordered as follows: dehydrogenases > urease > alkaline phosphatase > acid phosphatase. Cellulose added to soil (15 g kg-1) proved to be a good factor in the improvement of soil biochemical properties, although it did not limit the effects produced by zinc.
ACPase activity was localized in the apoplast of pea root nodules under phosphorus deficiency. Pea plants (Pisum sativum L. cv. Sześciotygodniowy) where inoculated with Rhizobium leguminosarum bv. viciae 248 and were cultured on nitrogen-free medium with phosphate (-N/+P) or phosphate-deficient (-N/-P) one. In comparison with control nodules, P-deficient nodules showed the increase of ACPase activity in plant cell walls and the infection threads. The increase in bacterial ACPase activtty under P-deficiency may reflect higher det mand for inorganic phosphorus that is necessary for bacteria multiplication within the infection threads. The increase of ACPase activity in nodule apoplast under P stress may enlarge the availability of phosphate for plant and bacteria.
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