Study on the inactivation of enzymes in Jerusalem artichoke tuber slices

1972 ◽  
Vol 50 (4) ◽  
pp. 727-731 ◽  
Author(s):  
Marcel Bastin ◽  
Osman Ünlüer
Keyword(s):  
Half Life ◽  
Jerusalem Artichoke ◽  
Phenol Oxidase ◽  
Enzyme Synthesis ◽  
Strong Inhibitor ◽  
First Order ◽  
Jerusalem Artichoke Tuber ◽  
Enzyme Degradation ◽  
Inhibitor Of Protein Synthesis ◽  
Stimulation Of

The formation of both peroxidase and phenol oxidase was induced by culturing slices of Jerusalem artichoke tubers under aerobic conditions at 30 °C. The rate of enzyme degradation in the tuber slices was measured after applying cycloheximide, a strong inhibitor of protein synthesis, or by culturing the tissues under anaerobic conditions. Peroxidase decayed according to a first order process with a half-life of 8.3 h while phenol oxidase was found to be more stable (half-life about 70 h). The increase in the level of enzymes after the slicing treatment was achieved through a stimulation of the rate of enzyme synthesis rather than a decrease in the rate of destruction.

Oxidation processes in relation to the induction of enzymes in Jerusalem artichoke tuber slices

1970 ◽  
Vol 48 (3) ◽  
pp. 316-321 ◽  
Author(s):  
Marcel Bastin ◽  
Huguette Dijkmans
Keyword(s):  
Oxygen Uptake ◽  
Jerusalem Artichoke ◽  
Phenol Oxidase ◽  
Carbonyl Groups ◽  
Oxidation Processes ◽  
Jerusalem Artichoke Tuber ◽  
Induction Of Enzymes ◽  
Ethylenediamine Tetraacetate

The effect of diethyldithiocarbamate (DIECA) and ethylenediamine tetraacetate (EDTA) on the wounding-dependent induction of phenol oxidase and peroxidase in Jerusalem artichoke tuber slices has been investigated. DIECA which is a good inhibitor of oxidase reactions inhibits the induction of enzymes. EDTA which does not affect these reactions prevents the induction only at a concentration of 5 μmoles/ml. At a concentration of 1 μmole/ml, however, which stimulates the rate of oxygen uptake by the slices, EDTA also stimulates the induction of enzymes.The induction of enzymes was enhanced when slices were cultured in the presence of compounds having two neighboring carbonyl groups (dehydroascorbate, pyruvate, and oxalate).The rate of both induction and oxygen uptake increased with increasing intensity of slicing.

scholarly journals Regulation of S-adenosylmethionine decarboxylase by polyamines in Ehrlich ascites-carcinoma cells grown in culture

1980 ◽  
Vol 190 (3) ◽  
pp. 747-754 ◽  
Author(s):  
Leena Alhonen-Hongisto
Keyword(s):  
Half Life ◽  
Ehrlich Ascites Carcinoma ◽  
Enzyme Synthesis ◽  
Tumour Cells ◽  
Transcriptional Level ◽  
Decarboxylase Activity ◽  
Adenosylmethionine Decarboxylase ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Tumour ◽  
Stimulation Of

1. The mechanism of stimulation of S-adenosylmethionine decarboxylase (EC 4.1.1.50) activity by inhibitors of ornithine decarboxylase (EC 4.1.1.17), namely dl-α-difluoromethylornithine, 1,3-diaminopropane and 1,3-diaminopropan-2-ol, was studied in Ehrlich ascites-tumour cells grown in suspension cultures. 2. Difluoromethylornithine and diaminopropane, although decreasing the content of putrescine and spermidine, markedly stimulated adenosylmethionine decarboxylase activity after exposure of the cells to the drugs for 8h, whereas the effect of diaminopropanol only became apparent many hours later. In tumour cells exposed to any of the inhibitors, a close negative correlation existed between the activity of adenosylmethionine decarboxylase and the intracellular concentration of spermidine and/or spermidine plus spermine, suggesting that a depletion of higher polyamines triggered enhancement of adenosylmethionine decarboxylase activity. 3. The mechanism of difluoromethylornithine- and diaminopropane-induced stimulation of adenosylmethionine decarboxylase involved (a) a marked increase in the apparent half-life of the enzyme and (b) an induction of enhanced enzyme synthesis. Diaminopropanol seemed to act solely via an induction mechanism. 4. The increased adenosylmethionine decarboxylase activity elicited by difluoromethylornithine could be restored to control values by micromolar concentrations of exogenous spermidine and spermine in 4h and by putrescine in 22h. In addition to the natural polyamines, elevated adenosylmethionine decarboxylase activity could be repressed by 3,3′-iminodipropylamine, a close analogue of spermidine, but not by non-physiological diamines. 5. Addition of spermidine and actinomycin D to cultures treated with difluoromethylornithine produced a comparable decay of enhanced adenosylmethionine decarboxylase activity (with an apparent half-life of about 2.5h), whereas the effect of cycloheximide was much more rapid. The present results suggest that polyamines may regulate adenosylmethionine decarboxylase at the transcriptional level of gene expression.

In-vitro Kinetic Hydrolysis Study of Metronidazole Derivatives with Carvacrol and Eugenol Using Validated RP-HPLC Method

2020 ◽  
Vol 16 ◽  
Author(s):  
M. Alarjah
Keyword(s):  
Half Life ◽  
Hplc Method ◽  
Hydrolysis Rate ◽  
First Order ◽  
First Order Kinetics ◽  
Rp Hplc ◽  
Pharmacokinetic Properties ◽  
Pseudo First Order ◽  
Kinetic Hydrolysis

Background: Prodrugs principle is widely used to improve the pharmacological and pharmacokinetic properties of some active drugs. Much effort was made to develop metronidazole prodrugs to enhance antibacterial activity and or to improve pharmacokinetic properties of the molecule or to lower the adverse effects of metronidazole. Objective: In this work, the pharmacokinetic properties of some of monoterpenes and eugenol pro metronidazole molecules that were developed earlier were evaluated in-vitro. The kinetic hydrolysis rate constants and half-life time estimation of the new metronidazole derivatives were calculated using the validated RP-HPLC method. Method: Chromatographic analysis was done using Zorbbax Eclipse eXtra Dense Bonding (XDB)-C18 column of dimensions (250 mm, 4.6 mm, 5 μm), at ambient column temperature. The mobile phase was a mixture of sodium dihydrogen phosphate buffer of pH 4.5 and methanol in gradient elution, at 1ml/min flow rate. The method was fully validated according to the International Council for Harmonization (ICH) guidelines. The hydrolysis process carried out in an acidic buffer pH 1.2 and in an alkaline buffer pH 7.4 in a thermostatic bath at 37ºC. Results: The results followed pseudo-first-order kinetics. All metronidazole prodrugs were stable in the acidic pH, while they were hydrolysed in the alkaline buffer within a few hours (6-8 hr). The rate constant and half-life values were calculated, and their values were found to be 0.082- 0.117 hr-1 and 5.9- 8.5 hr., respectively. Conclusion: The developed method was accurate, sensitive, and selective for the prodrugs. For most of the prodrugs, the hydrolysis followed pseudo-first-order kinetics; the method might be utilised to conduct an in-vivo study for the metronidazole derivatives with monoterpenes and eugenol.

scholarly journals β-Adrenergic stimulation alters oligosaccharide pyrophosphoryl dolichol metabolism in rat parotid acinar cells

1985 ◽  
Vol 231 (2) ◽  
pp. 431-438 ◽  
Author(s):  
S R Grant ◽  
E E Kousvelari ◽  
D K Banerjee ◽  
B J Baum
Keyword(s):  
Half Life ◽  
Specific Radioactivity ◽  
Acinar Cells ◽  
Protein Glycosylation ◽  
Significant Enhancement ◽  
Adrenergic Stimulation ◽  
Parotid Acinar Cells ◽  
Secretory Glycoproteins ◽  
Rat Parotid ◽  
Stimulation Of

beta-Adrenergic stimulation of rat parotid acinar cells markedly increases [3H]mannose incorporation into N-linked glycoproteins [Kousvelari, Grant, Banerjee, Newby & Baum (1984) Biochem. J. 222, 17-24]. More than 90% of this protein-bound [3H]mannose was preferentially incorporated into four secretory glycoproteins. The ratio of [3H]mannose/[14C]leucine present in these individual proteins was 1.7-4-fold greater with isoproterenol-treated cells than with untreated controls. In isoproterenol-stimulated cells, [3H]mannose incorporation into mannosylphosphoryl dolichol and oligosaccharide-PP-dolichol was increased 2-3-fold over that observed in unstimulated cells. Similarly, formation of mannosylated oligosaccharide-PP-dolichol was increased approx. 4-fold in microsomes prepared from isoproterenol-treated cells. Also, turnover of oligosaccharide-PP-dolichol was significantly increased (5-fold) by β-adrenergic stimulation; the half-life for oligosaccharide-PP-dolichol decreased from 6 min in control cells to 1.2 min in isoproterenol-stimulated cells. By 15 min after isoproterenol addition to acinar cells, the specific radioactivity of parotid oligosaccharide moieties increased about 3-fold over the value observed in the absence of the agonist. Taken together, these results strongly suggest that elevation of N-linked protein glycosylation in rat parotid acinar cells after β-adrenoreceptor stimulation resulted from significant enhancement in the synthesis of mannosylphosphoryl dolichol and oligosaccharide-PP-dolichol and the turnover of oligosaccharide-PP-dolichol.

Observation of a radical intermediate in the one electron oxidation of 5-methyl-1-thia-5-azacyclooctane by •Br2−

1984 ◽  
Vol 62 (9) ◽  
pp. 1874-1876 ◽  
Author(s):  
Warren Kenneth Musker ◽  
Parminder S. Surdhar ◽  
Rizwan Ahmad ◽  
David A. Armstrong
Keyword(s):  
Aqueous Solution ◽  
Rate Constant ◽  
Half Life ◽  
Cation Radical ◽  
Order Rate Constant ◽  
Type Structure ◽  
Radical Intermediate ◽  
Text Type ◽  
First Order ◽  
The One

The one electron oxidant •Br2− reacts with 5-methyl-1-thia-5-azacyclooctane (4) in aqueous solution at high pH with an overall rate constant of ~2 × 108 M s−1. The radical intermediate produced has a broad maximum at 500 nm with ε = 2400 M−1 cm−1 and at pH 10 decays with a first order rate constant of 2.3 ± 0.3 × 104 s−1, first half-life of 30 ± 5 μs. Its characteristics do not correspond to those of the [Formula: see text] species reported by Asmus and co-workers. The species appears to be the same as the cation radical reported earlier in the one electron oxidation of 4 in acetonitrile. This species is considered to have an [Formula: see text] type structure, which provides transannular stabilization.

Pharmacokinetics and Tolerability of a New Low Molecular Mass Heparin (RO-11) in Healthy Volunteers – A Dose-Finding Study within the Therapeutical Range

1997 ◽  
Vol 77 (01) ◽  
pp. 133-136 ◽  
Author(s):  
Liliana Falkon ◽  
Miriam M Bayés ◽  
Guillem Frontera ◽  
Mercè Garí ◽  
Manel Barbanoj ◽  
...  
Keyword(s):  
Phase I ◽  
Molecular Mass ◽  
Half Life ◽  
Dose Finding ◽  
Dose Effect ◽  
Efficacy And Safety ◽  
First Order ◽  
Finding Study ◽  
Dose Finding Study ◽  
Dose Dependent

SummaryThis paper reports on the results of a Phase I, dose-finding study with a new low molecular mass heparin (LMMH) called RO-11. The study focused on pharmacokinetics, dose-effect relationship and on tolerability of three single subcutaneous (SC) doses within the therapeutical range. After the injection of 7,500, 9,000 and 12,500 anti-FXa IU, the anti-FXa effect peaked between 3-6 h and showed a dose-dependent response. The absorption and elimination were first-order processes and the long half-life (>5 h) kept constant after increasing doses. The compound was tolerated very well and no clinically relevant prolongation of APTT, prothrombin and thrombin clotting tests was observed. At the dose of 7,500 IU, which corresponded to 110 anti-FXa IU/Kg, RO-11 exerted anti-FXa effect for at least 18-20 h. We recommend using this dose in a single SC injection, to evaluate the efficacy and safety of RO-11 in the initial treatment of DVT or PE.

Use of purified lyophilized human lactate dehydrogenase isoenzyme 5 in a study of measuring lactate dehydrogenase activity.

1989 ◽  
Vol 35 (8) ◽  
pp. 1774-1776 ◽  
Author(s):  
D A Smith ◽  
G C Moses ◽  
A R Henderson
Keyword(s):  
Lactate Dehydrogenase ◽  
Half Life ◽  
Specific Activity ◽  
Lactate Dehydrogenase Activity ◽  
Bovine Albumin ◽  
First Order ◽  
First Order Kinetics ◽  
The Stability ◽  
Lactate Dehydrogenase Isoenzymes ◽  
Excellent Stability

Abstract We examined the stability of human lactate dehydrogenase (EC 1.1.1.27) isoenzyme 5--purified to a specific activity of about 400 kU/g--when lyophilized in a buffered, stabilized matrix of bovine albumin. This isoenzyme was prepared with a final activity of about 500 U/L and stored at -20, 4, 20, 37, and 56 degrees C for as long as six months. This isoenzyme decayed with approximate first-order kinetics, with an estimated half-life at -20 degrees C of about 475 years. Stability of reconstituted samples stored at 20 or 4 degrees C was poor, suggesting that the reconstituted material should be used without delay; material stored at -20 degrees C showed excellent stability for 15 days. We propose that such preparations might be further investigated as standards for use in electrophoresis of lactate dehydrogenase isoenzymes.

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