Phosphatase systems in Fasciolopsis buski Lankester, 1857 and Gastrodiscus aegyptiacus Cobbold, 1876

Parasitology ◽  
1973 ◽  
Vol 67 (2) ◽  
pp. 197-204 ◽  
Author(s):  
Madan M. Goil
Keyword(s):  
Enzyme Activity ◽  
Tartaric Acid ◽  
Maximum Activity ◽  
Nitrophenyl Phosphate ◽  
Biochemical Studies ◽  
Phosphate Hydrolysis ◽  
Fasciolopsis Buski ◽  
Enzyme I ◽  
Inhibited Enzyme ◽  
Acid Phosphomonoesterase

Biochemical studies on the non-specific phosphomonoesterases have demonstrated the presence of acid phosphomonoesterase with maximum activity at pH 4·0 in Gastrodiscus aegyptiacus (enzyme I) and at pH 4·5 in the case of Fasdolopsis buski (enzyme II). The Km for ρ-nitrophenyl phosphate hydrolysis was 0·66 mM for enzyme I and 1·1 mM for enzyme II. Different concentrations of fluoride, arsenate, tartrate, tartaric acid, cysteine and copper brought about inhibition of both enzymes and magnesium, iodoaeetate, iodoacetamide and EDTA had no influence on either enzyme activity. Cobalt activated both enzymes while zinc inhibited enzyme I and strongly stimulated enzyme II.

The effect of five fasciolicides on malate dehydrogenase activity and mortality of Fasciola gigantica, Fasciolopsis buski and Paramphistomum explanatum

1981 ◽  
Vol 55 (2) ◽  
pp. 115-122 ◽  
Author(s):  
A. J. Probert ◽  
R. K. Sharma ◽  
K. Singh ◽  
R. Saxena
Keyword(s):  
Enzyme Activity ◽  
Dehydrogenase Activity ◽  
Malate Dehydrogenase ◽  
Fasciola Gigantica ◽  
High Concentrations ◽  
Fasciolopsis Buski ◽  
Reduced Activity ◽  
Inhibited Enzyme ◽  
Malate Oxidation

ABSTRACTThe effect of oxyclozanide, hexachlorophene, nitroxynil, rafoxanide and diamphenethide on malate dehydrogenase activity of homogenates of Fasciola gigantica, Fasciolopsis buski and Paramphistomum explanatum was investigated. The ratio of oxaloacetate reduction to malate oxidation in homogenates of Fasciola gigantica, Fasciolopsis buski and P. explanatum was 4·5:1, 3·6:1 and 5·2:1 respectively. Oxyclozanide and rafoxanide at 10−3 M inhibited enzyme activity by 100% in homogenates from all three species while hexachlorophene at 10−3M also caused 100% inhibition in homogenates from Fasciola gigantica and P. explanatum but only 65% of malate oxidation in Fasciolopsis buski homogenates. Nitroxynil at 10−3M produced 60% inhibition in F. buski homogenates yet had little effect at this concentration on preparations from the other species. Little inhibition was seen with diamphenethide, even at high concentrations. Rapid death of Fasicola gigantica and P. explanatum resulted in vitro when 10−3M oxyclozanide, hexachlorophene, nitroxynil or rafoxanide, were added to the incubation medium. Fasciolopsis buski was killed by 10−3M oxyclozanide but at this concentration the remaining compounds only caused reduced activity. Assay of malate dehydrogenase following drug treatment in vitro failed to show any appreciable reduction in enzyme activity in Fasciola gigantica and P. explanatum but oxyclozanide and hexachlorophene produced inhibition in Fasciolopsis buski. The mode of action of these compounds is discussed.

Non-specific alkaline phosphomonoesterases of eight species of digenetic trematodes

1975 ◽  
Vol 49 (4) ◽  
pp. 281-287 ◽  
Author(s):  
Wajih A. Nizami ◽  
Ather H. Siddiqi ◽  
A. N. K. Yusufi
Keyword(s):  
Enzyme Activity ◽  
Bubalus Bubalis ◽  
Alkaline Phosphatases ◽  
Gastrothylax Crumenifer ◽  
Digenetic Trematodes ◽  
Wallago Attu ◽  
Fasciolopsis Buski ◽  
Two Peaks ◽  
Different Levels ◽  
Inhibited Enzyme

ABSTRACTAlkaline phosphatases from different trematodes occupying the same habitat have identical pH optima but different levels of enzyme activities. Isoparorchis hypselobagri, from the fish Wallago attu, shows four to six times more enzyme activity than Fasciolopsis buski, Gastrodiscoides hominis and Echinostoma malayanum, from the pig Sus scrofa, and Fasciola gigantica, Gigantocotyle explanatum, Cotylophoron cotylophorum and Gastrothylax crumenifer, from the buffalo Bubalus bubalis.At least two peaks of activity at different levels of pH were obtained for each trematode examined. Both Gastrodiscoides hominis and Isoparorchis hypselobagri enzymes had three peaks of alkaline phosphatase activity.The optimum temperature for maximum enzyme activity was 40°C, above which rapid inactivation occurred. At temperatures below 40°C, the enzymes of fish and mammalian trematodes did not behave similarly; I. hypselobagri enzyme being active over a wider range of temperature (20°–40°C.Various concentrations of KCN and arsenate proportionately inhibited enzyme activity. NaF did not significantly influence enzyme activity, while Mg++ and CO++ acted as activators. The extent of inhibition or activation of enzyme activity of different trematodes varied, probably due to species differences. Both inhibition and activation of I. hypselobagri enzyme was higher than in the case of other trematodes.

Inorganic pyrophosphatase from Ferrobacillus ferrooxidans (Thiobacillus ferrooxidans)

1970 ◽  
Vol 48 (12) ◽  
pp. 1302-1307 ◽  
Author(s):  
Adele Howard ◽  
D. G. Lundgren
Keyword(s):  
Enzyme Activity ◽  
Thiobacillus Ferrooxidans ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Maximum Activity ◽  
Inorganic Pyrophosphatase ◽  
Ph Optimum ◽  
Heat Stable ◽  
Nitrophenyl Phosphate ◽  
Binding Agents

An inorganic pyrophosphatase was isolated from Ferrobacillus ferrooxidans and purified 21-fold. The cation Mg2+ was required for maximum activity; Mn2+, Zn2+, and Co2+ supported less than 10% of the activity with Mg2+. The pH optimum of the enzyme was between 7.5 and 8.5, using a magnesium to pyrophosphate ratio of one. The purified enzyme was unable to hydrolyze adenosine triphosphate, adenosine diphosphate, adenosine monophosphate, or various other monophosphates; p-nitrophenyl-phosphate, the substrate for alkaline pyrophosphatase, was not hydrolyzed. Sulfhydryl binding agents did not inhibit enzyme activity, and the enzyme, in the presence of Mg2+, was heat-stable.

scholarly journals Partial purification and biochemical characterization of a new highly acidic NYSO laccase from Alcaligenes faecalis

2020 ◽  
Vol 18 (1) ◽  
Author(s):  
Soad A. Abdelgalil ◽  
Ahmad R. Attia ◽  
Reyed M. Reyed ◽  
Nadia A. Soliman
Keyword(s):  
Enzyme Activity ◽  
Sodium Dodecyl ◽  
Alcaligenes Faecalis ◽  
Maximum Activity ◽  
Sodium Oxalate ◽  
Partial Purification ◽  
Bromophenol Blue ◽  
Bromocresol Purple ◽  
Laccase Enzyme

Abstract Background Due to the multitude industrial applications of ligninolytic enzymes, their demands are increasing. Partial purification and intensive characterization of contemporary highly acidic laccase enzyme produced by an Egyptian local isolate designated Alcaligenes faecalis NYSO were studied in the present investigation. Results Alcaligenes faecalis NYSO laccase has been partially purified and intensively biochemically characterized. It was noticed that 40–60% ammonium sulfate saturation showed maximum activity. A protein band with an apparent molecular mass of ~ 50 kDa related to NYSO laccase was identified through SDS-PAGE and zymography. The partially purified enzyme exhibited maximum activity at 55 °C and pH suboptimal (2.5–5.0). Remarkable activation for enzyme activity was recognized after 10-min exposure to temperatures (T) 50, 60, and 70 °C; time elongation caused inactivation, where ~ 50% of activity was lost after a 7-h exposure to 60 °C. Some metal ions Cu2+, Zn2+, Co2+, Ni2+, Mn2+, Cd2+, Cr2+, and Mg2+ caused strong stimulation for enzyme activity, but Fe2+ and Hg2+ reduced the activity. One millimolar of chelating agents [ethylenediamine tetraacetic acid (EDTA), sodium citrate, and sodium oxalate] caused strong activation for enzyme activity. Sodium dodecyl sulfate (SDS), cysteine-HCl, dithiothreitol (DTT), β-mercaptoethanol, thioglycolic acid, and sodium azide caused strong inhibition for NYSO laccase activity even at low concentration. One millimolar of urea, imidazole, kojic acid, phenylmethylsulfonyl fluoride (PMSF), H2O2, and Triton X-100 caused activation. The partially purified NYSO laccase had decolorization activity towards different dyes such as congo red, crystal violet, methylene blue, fast green, basic fuchsin, bromophenol blue, malachite green, bromocresol purple eriochrome black T, and Coomassie Brilliant Blue R-250 with various degree of degradation. Also, it had a vast range of substrate specificity including lignin, but with high affinity towards p-anisidine. Conclusion The promising properties of the newly studied laccase enzyme from Alcaligenes faecalis NYSO strain would support several industries such as textile, food, and paper and open the possibility for commercial use in water treatment. It will also open the door to new applications due to its ligninolytic properties in the near future.

An Investigation of the Histochemical Technique for the Localization of Acid Phosphomonoesterase

1950 ◽  
Vol s3-91 (15) ◽  
pp. 315-330
Author(s):  
FRANCES MACDONALD
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Standard Technique ◽  
Formalin Fixation ◽  
Histochemical Technique ◽  
Acid Phosphomonoesterase

1. A method is described for assessing the depth of ‘staining’ obtained with the acid phosphatase technique and a detailed scheme is given of the standard technique used. 2. It is concluded that the technique specifically demonstrates the activity of acid phosphatase, since ‘staining’ is abolished in the absence of substrate, in heated sections, and in the presence of fluoride. 3. An investigation has been carried out to determine the extent to which the reaction is affected by altering various stages in the technique. 4. The effect of formalin fixation on the reaction has been investigated. 5. It has been shown that sites in the rabbit medulla having an affinity for the reagents used in the technique differ from the sites at which a precipitate is deposited as a result of enzyme activity. 6. Evidence is presented suggesting that the technique may not demonstrate the true physiological localization of the enzyme. 7. It is suggested that the technique may be of value as a neurohistological method.

Coenzyme A metabolism

1985 ◽  
Vol 248 (1) ◽  
pp. E1-E9 ◽  
Author(s):  
J. D. Robishaw ◽  
J. R. Neely
Keyword(s):  
Enzyme Activity ◽  
Cardiac Muscle ◽  
Heart Muscle ◽  
Coenzyme A ◽  
Free Carnitine ◽  
Pantothenate Kinase ◽  
Acetyl Coenzyme A ◽  
Synthetic Pathway ◽  
And Control ◽  
Inhibited Enzyme

The metabolism of coenzyme A and control of its synthesis are reviewed. Pantothenate kinase is an important rate-controlling enzyme in the synthetic pathway of all tissues studied and appears to catalyze the flux-generating reaction of the pathway in cardiac muscle. This enzyme is strongly inhibited by coenzyme A and all of its acyl esters. The cytosolic concentrations of coenzyme A and acetyl coenzyme A in both liver and heart are high enough to totally inhibit pantothenate kinase under all conditions. Free carnitine, but not acetyl carnitine, deinhibits the coenzyme A-inhibited enzyme. Carnitine alone does not increase enzyme activity. Thus changes in the acetyl carnitine-to-carnitine ratio that occur with nutritional states provides a mechanism for regulation of coenzyme A synthetic rates. Changes in the rate of coenzyme A synthesis in liver and heart occurs with fasting, refeeding, and diabetes and in heart muscle with hypertrophy. The pathway and regulation of coenzyme A degradation are not understood.

Physiological studies on trematodes: phosphatase systems in Gastrothylax crumenifer

Parasitology ◽  
1966 ◽  
Vol 56 (1) ◽  
pp. 105-110 ◽  
Author(s):  
Madan M. Goil
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Maximum Activity ◽  
Fluoride Ions ◽  
Gastrothylax Crumenifer ◽  
Biochemical Studies ◽  
Physiological Studies ◽  
Phosphatase Enzyme

Biochemical studies on the phosphatase systems of Gastrothylax crumenifer have been made. The maximum activity of the phosphatase enzyme was found to be at 5 pH. The action of magnesium and fluoride ions on the acid phosphatase activity shows that both act as inhibitors. The day-to-day variation in the phosphatase activity of the samples, as measured by block differences, was found to be significant at different pH levels. The heat denatured extract showed low and fairly constant acid phosphatase activity.

ÉTUDE DES EFFETS ÉLECTROSTATIQUES SUR LE MÉCANISME D'ACTION CATALYTIQUE DE LA PHOSPHATASE ALCALINE INTESTINALE DE VEAU

1965 ◽  
Vol 43 (8) ◽  
pp. 2222-2235 ◽  
Author(s):  
Michel Lazdunski ◽  
Jacques Brouillard ◽  
Ludovic Ouellet
Keyword(s):  
Dielectric Constant ◽  
Ionic Strength ◽  
Maximum Activity ◽  
Enzyme Molecule ◽  
High Substrate Concentration ◽  
Nitrophenyl Phosphate ◽  
Phosphatase Alcaline ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of ◽  
Activated Complex

The influence of dioxane and ethanol on the rate of hydrolysis of p-nitrophenyl phosphate in the presence of an intestinal alcaline phosphatase can be interpreted as a dielectric constant effect, at high substrate concentration. The dielectric constant effect is a function of the pH of the medium and is maximum around pH 9.4 at 25 °C and pH 9.0 at 15 °C. An interpretation suggesting that the change in diameter of the enzyme molecule becoming an activated complex is minimum at a pH of maximum activity is proposed. The same model can take into account the influence of the ionic strength on the same reaction.

scholarly journals Isolation of Bacillus spp. Bacteria from Soil for Production of Cellulase

2019 ◽  
Vol 6 (1) ◽  
pp. 57-61 ◽  
Author(s):  
Amika Ahmed Manzum ◽  
Md Arafat Al Mamun
Keyword(s):  
Enzyme Activity ◽  
Genetic Improvement ◽  
Test Tube ◽  
Maximum Activity ◽  
Soil Samples ◽  
Shake Culture ◽  
Good Source ◽  
Tube Culture ◽  
Bacillus Spp ◽  
Food And Feed

Cellualse is one of the most important enzymes used in textile, detergent, paper, food and feed industries. Therefore, a study was undertaken to isolate Bacillus bacteria having the potential to produce cellulase from soil samples. 24 soil samples were analyzed and 54 presumptive Bacillus isolates were isolated after heating the soil samples at 80°C for 10 min. Among them 45 isolates showed enzyme activity ranging from 0.003 to 0.17 U/ml in test tubes containing 5 ml medium composed of (g/L) glucose 0.5 gm, peptone 0.75 gm, FeSO4 0.01 gm, KH2PO4 0.5 gm, and MgSO4 0.5 gm at 120 rpm, 37° C and pH 7. Among them 1RW, 2WS, 3YR, 4WT, 6 RR, and 9SS showed 0.17, 0.15, 0.14, 0.15, 0.147 and 0.14U/ml enzyme activities, respectively. Production of cellulase by these isolates was further scaled up to shake culture containing 50 ml medium similar to that used in test tube culture. Among the isolates 1 RW showed the maximum activity. This 1 RW was identified by API kit and showed that 59 % belongs to Bacillus licheniformis strain (51% confirmation) or Bacillus subtilis (31% confirmation). Further gene analysis is required to confirm the species. The genetic improvement study will make the isolate a good source of cellulase.

Development of Isocitric Lyase Activity in Germinating Prickly Sida Seed

Weed Science ◽  
1976 ◽  
Vol 24 (3) ◽  
pp. 298-301 ◽  
Author(s):  
Bonnie J. Reger ◽  
E. Wayne Smith
Keyword(s):  
Enzyme Activity ◽  
Actinomycin D ◽  
Maximum Activity ◽  
Lyase Activity ◽  
Radicle Protrusion ◽  
Sida Spinosa ◽  
D 12 ◽  
Prickly Sida

Maximum activity of isocitric lyase (EC 4.1.3.1) was reached at 24 hr incubation of afterripened (nondormant) prickly sida (Sida spinosaL.) seed. Enzyme activity declined gradually with incubation times in excess of 24 hr. Actinomycin D (Act D) at 5 μg/ml had essentially no effect on 24-hr germination but inhibited development of isocitric lyase activity 83%. Cycloheximide (CH) at 10 μg/ml inhibited 24-hr germination of punctured seed only 7% but inhibited development of isocitric lyase activity 76%. Seed incubated in water 12 hr before being transferred to Act D at 5 μg/ml for an additional 12 hr did not escape sensitivity to the antibiotic. Isocitric lyase activity was inhibited when assayed at 24 hr total incubation. In the reverse experiment, seed incubated in Act D 12 hr before being transferred to water, isocitric lyase activity at 24 hr was not affected. Apparently prickly sida seed lacked a performed mRNA for isocitric lyase and transcription and translation of the mRNA occurred shortly after initiation of radicle protrusion (~8 hr).

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