scholarly journals A rapid simple method for the assay of renin in rabbit plasma

1968 ◽  
Vol 108 (4) ◽  
pp. 679-685 ◽  
Author(s):  
J W Ryan ◽  
J. K. McKenzie ◽  
M. R. Lee
Keyword(s):  
Rabbit Plasma ◽  
Selective Inhibitors ◽  
Angiotensin I ◽  
Simple Method ◽  
Renin Substrate ◽  
First Order ◽  
Complete Inactivation ◽  
Plasma Enzymes ◽  
First Order Kinetics ◽  
Percentage Release

1. EDTA (10mm), 2,3-dimercaptopropan-1-ol (10mm) and chlorhexidine gluconate (0·005%, w/v) cause complete inactivation of plasma enzymes that degrade angiotensin I, but have no effect on the reaction of renin with its substrate. The reagents were termed the selective inhibitors. 2. Thus it is possible to measure renin in plasma by its ability to catalyse the release of angiotensin I. 3. Sterile plasma, treated with the selective inhibitors, is incubated with renin substrate (500–1000ng. of angiotensin content/ml.) at pH6 at 42° for 6hr. 4. Under these conditions the reaction obeys first-order kinetics. Renin activity is calculated in terms of the percentage release of the angiotensin content/hr. 5. As described, the assay is sufficiently sensitive to measure renin in the plasma of all normal rabbits. By extending the length of the incubation, much lower activities can be measured.

scholarly journals Properties of renin substrate in rabbit plasma with a note on its assay

1968 ◽  
Vol 108 (4) ◽  
pp. 687-692 ◽  
Author(s):  
J W Ryan ◽  
J. K. McKenzie
Keyword(s):  
Substrate Concentration ◽  
Rabbit Plasma ◽  
Selective Inhibitors ◽  
Angiotensin I ◽  
Renin Substrate ◽  
First Order ◽  
Plasma Enzymes ◽  
First Order Kinetics ◽  
Time Required ◽  
Substrate Concentrations

1. Rabbit plasma enzymes that degrade angiotensin I are inhibited completely by the combination of 2,3-dimercaptopropan-1-ol (10mm), EDTA (10mm) and chlorhexidine gluconate (0·005%, w/v). These compounds do not modify the reaction of renin with renin substrate and are termed the selective inhibitors. 2. The renin substrate concentration of plasma can be measured as angiotensin I content by incubating plasma plus the selective inhibitors with renin for a time sufficient to allow complete utilization of renin substrate. 3. This reaction obeys first-order kinetics to substrate concentrations of at least 1000ng. of angiotensin I content/ml. In general, the renin substrate concentrations of normal rabbit plasmas are less than 1000ng. of angiotensin I content/ml. Thus the time required for the complete release of angiotensin I from normal plasma is inversely related to renin activity and is independent of renin substrate concentration. 4. A method for the assay of renin substrate, taking these reaction kinetics into account, is presented.

scholarly journals A KINETIC ANALYSIS OF THE RENIN-ANGIOTONIN PRESSOR SYSTEM AND THE STANDARDIZATION OF THE ENZYMES RENIN AND ANGIOTONASE

1943 ◽  
Vol 78 (5) ◽  
pp. 367-386 ◽  
Author(s):  
Albert A. Plentl ◽  
Irvine H. Page
Keyword(s):  
Pressor Response ◽  
Accurate Method ◽  
Enzyme Concentration ◽  
Renin Substrate ◽  
First Order ◽  
First Order Kinetics ◽  
Consecutive Reactions ◽  
Slow Decline ◽  
Reaction Constant

The physicochemical background of the renal vasporessor system (renin-renin-substrate, angiotinin, angiotonase) is given. The formation and destruction of angiotonin is shown to consist of two consecutive reactions, both of which follow the laws of first order kinetics. Each reaction was studied separately and its reaction constant found to be proportional to the enzyme concentration. Hence these constants should be used to express the activity of the enzymes, renin and angiotonase. The over-all reaction of a mixture of renin and angiotonase such as occurs in kidney extracts with the α-globulin fraction of serum, viz., rapid increase followed by a slow decline in angiotonin concentration, was found experimentally to correspond closely to the theoretical values calculated for such a reaction. The curve obtained also satisfyingly explains the characteristic pressor response to the intravenous injection of renin. An accurate method for the determination of renin in the presence of angiotonase is presented.

Inhibition of E. coli ʟ-Asparaginase by Reaction with 2,3-Butanedione. Chemical Modification of Arginine and Histidine Residues

1979 ◽  
Vol 34 (9-10) ◽  
pp. 742-746 ◽  
Author(s):  
Dorothee Petz ◽  
Hans-Gerhard Löffler ◽  
Friedh. Schneider
Keyword(s):  
Chemical Modification ◽  
Histidine Modification ◽  
Histidine Residues ◽  
E Coli ◽  
First Order ◽  
Complete Inactivation ◽  
First Order Kinetics ◽  
Competitive Inhibitors ◽  
Pseudo First Order

Abstract The inactivation of E. coli asparaginase by 2,3-butanedione studied with ʟ-asparagine and diazooxonorvaline as substrates obeys pseudo first order kinetics. Activity losses are linear with respect to arginine and histidine modification, with complete inactivation being correlated with alteration of one arginine and one histidine per subunit. The rate of inactivation of the enzym was reduced in the presence of competitive inhibitors like ʟ-2-amino-2-carboxyethane-sulfonamide. Un der comparable conditions 1,2-cyclo hexanedione does not affect the activity of ʟ-asparaginase.

scholarly journals Evidence for an essential arginine residue at the active site of ATP citrate lyase from rat liver

1981 ◽  
Vol 195 (3) ◽  
pp. 735-743 ◽  
Author(s):  
S Ramakrishna ◽  
W B Benjamin
Keyword(s):  
Rat Liver ◽  
Active Site ◽  
Arginine Residue ◽  
Atp Citrate Lyase ◽  
First Order ◽  
Complete Inactivation ◽  
First Order Kinetics ◽  
Citrate Lyase ◽  
Arginine Residues ◽  
Pseudo First Order

Rat liver ATP citrate lyase was inactivated by 2, 3-butanedione and phenylglyoxal. Phenylglyoxal caused the most rapid and complete inactivation of enzyme activity in 4-(2-hydroxyethyl)-1-piperazine-ethanesulphonic acid buffer, pH 8. Inactivation by both butanedione and phenylglyoxal was concentration-dependent and followed pseudo- first-order kinetics. Phenylglyoxal also decreased autophosphorylation (catalytic phosphate) of ATP citrate lyase. Inactivation by phenylglyoxal and butanedione was due to the modification of enzyme arginine residues: the modified enzyme failed to bind to CoA-agarose. The V declined as a function of inactivation, but the Km values were unaltered. The substrates, CoASH and CoASH plus citrate, protected the enzyme significantly against inactivation, but ATP provided little protection. Inactivation with excess reagent modified about eight arginine residues per monomer of enzyme. Citrate, CoASH and ATP protected two to three arginine residues from modification by phenylglyoxal. Analysis of the data by statistical methods suggested that the inactivation was due to modification of one essential arginine residue per monomer of lyase, which was modified 1.5 times more rapidly than were the other arginine residues. Our results suggest that this essential arginine residue is at the CoASH binding site.

A simple method for analyzing first-order kinetics

1990 ◽  
Vol 67 (6) ◽  
pp. 459 ◽  
Author(s):  
B. Borderie ◽  
D. Lavabre ◽  
G. Levy ◽  
J. C. Micheau
Keyword(s):  
Simple Method ◽  
First Order ◽  
First Order Kinetics

Photo-catalytic degradation of gaseous pollutants in paper mills of southern China

TAPPI Journal ◽  
2018 ◽  
Vol 17 (03) ◽  
pp. 167-178 ◽  
Author(s):  
Xin Tong ◽  
Jiao Li ◽  
Jun Ma ◽  
Xiaoquan Chen ◽  
Wenhao Shen
Keyword(s):  
Degradation Rate ◽  
Southern China ◽  
Catalytic Degradation ◽  
Pulp And Paper ◽  
Gaseous Pollutants ◽  
Pulp And Paper Mills ◽  
Paper Mills ◽  
Initial Concentration ◽  
First Order ◽  
First Order Kinetics

Studies were undertaken to evaluate gaseous pollutants in workplace air within pulp and paper mills and to consider the effectiveness of photo-catalytic treatment of this air. Ambient air at 30 sampling sites in five pulp and paper mills of southern China were sampled and analyzed. The results revealed that formaldehyde and various benzene-based molecules were the main gaseous pollutants at these five mills. A photo-catalytic reactor system with titanium dioxide (TiO2) was developed and evaluated for degradation of formaldehyde, benzene and their mixtures. The experimental results demonstrated that both formaldehyde and benzene in their pure forms could be completely photo-catalytic degraded, though the degradation of benzene was much more difficult than that for formaldehyde. Study of the photo-catalytic degradation kinetics revealed that the degradation rate of formaldehyde increased with initial concentration fitting a first-order kinetics reaction. In contrast, the degradation rate of benzene had no relationship with initial concentration and degradation did not conform to first-order kinetics. The photo-catalytic degradation of formaldehyde-benzene mixtures indicated that formaldehyde behaved differently than when treated in its pure form. The degradation time was two times longer and the kinetics did not reflect a first-order reaction. The degradation of benzene was similar in both pure form and when mixed with formaldehyde.

Kinetic of oxidation of methyl orange by vanadium(V) under conditions VO2+ and decavanadates coexist: Catalysis by Triton X-100 micellar medium

2019 ◽  
Author(s):  
Chem Int
Keyword(s):  
Methyl Orange ◽  
Solution Ph ◽  
Vanadium Concentration ◽  
Limiting Behavior ◽  
First Order ◽  
First Order Kinetics ◽  
Ph Range ◽  
Kinetic Pattern ◽  
Triton X ◽  
Kinetics Of

The kinetics of oxidation of methyl orange by vanadium(V) {V(V)} has been investigated in the pH range 2.3-3.79. In this pH range V(V) exists both in the form of decavanadates and VO2+. The kinetic results are distinctly different from the results obtained for the same reaction in highly acidic solution (pH < 1) where V(V) exists only in the form of VO2+. The reaction obeys first order kinetics with respect to methyl orange but the rate has very little dependence on total vanadium concentration. The reaction is accelerated by H+ ion but the dependence of rate on [H+] is less than that corresponding to first order dependence. The equilibrium between decavanadates and VO2+ explains the different kinetic pattern observed in this pH range. The reaction is markedly accelerated by Triton X-100 micelles. The rate-[surfactant] profile shows a limiting behavior indicative of a unimolecular pathway in the micellar pseudophase.

Biodegradation rates of aromatic contaminants in biofilm reactors

1995 ◽  
Vol 31 (1) ◽  
pp. 117-128 ◽  
Author(s):  
Jean-Pierre Arcangeli ◽  
Erik Arvin
Keyword(s):  
Aromatic Hydrocarbons ◽  
Competitive Inhibition ◽  
Removal Rate ◽  
First Order ◽  
Biofilm Reactors ◽  
First Order Kinetics ◽  
Reducing Conditions ◽  
Low Concentrations ◽  
Degradation Rates ◽  
Order Surface

This study has shown that microorganisms can adapt to degrade mixtures of aromatic pollutants at relatively high rates in the μg/l concentration range. The biodegradation rates of the following compounds were investigated in biofilm systems: aromatic hydrocarbons, phenol, methylphenols, chlorophenols, nitrophenol, chlorobenzenes and aromatic nitrogen-, sulphur- or oxygen-containing heterocyclic compounds (NSO-compounds). Furthermore, a comparison with degradation rates observed for easily degradable organics is also presented. At concentrations below 20-100 μg/l the degradation of the aromatic compounds was typically controlled by first order kinetics. The first-order surface removal rate constants were surprisingly similar, ranging from 2 to 4 m/d. It appears that NSO-compounds inhibit the degradation of aromatic hydrocarbons, even at very low concentrations of NSO-compounds. Under nitrate-reducing conditions, toluene was easily biodegraded. The xylenes and ethylbenzene were degraded cometabolically if toluene was used as a primary carbon source; their removal was influenced by competitive inhibition with toluene. These interaction phenomena are discussed in this paper and a kinetic model taking into account cometabolism and competitive inhibition is proposed.

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.

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