Enzymatic colorimetry of lecithin and sphingomyelin in aqueous solution.

1983 ◽  
Vol 29 (8) ◽  
pp. 1513-1517 ◽  
Author(s):  
M W McGowan ◽  
J D Artiss ◽  
B Zak
Keyword(s):  
Aqueous Solution ◽  
Hydrogen Peroxide ◽  
Amniotic Fluid ◽  
Enzymatic Reaction ◽  
Detergent Solution ◽  
Enzymatic Determination ◽  
Red Color ◽  
Hydrolysis Of ◽  
Zwitterionic Detergent

Abstract A procedure for the enzymatic determination of lecithin and sphingomyelin in aqueous solution is described. The phospholipids are first dissolved in chloroform:methanol (2:1 by vol), the solvent is evaporated, and the residue is redissolved in an aqueous zwitterionic detergent solution. The enzymatic reaction sequences of both assays involve hydrolysis of the phospholipids to produce choline, which is then oxidized to betaine, thus generating hydrogen peroxide. The hydrogen peroxide is subsequently utilized in the enzymatic coupling of 4-aminoantipyrine and sodium 2-hydroxy-3,5-dichlorobenzenesulfonate, an intensely red color being formed. The presence of a non-reacting phospholipid enhances the hydrolysis of the reacting phospholipid. Thus we added lecithin to the sphingomyelin standards and sphingomyelin to the lecithin standards. This precise procedure may be applicable to determination of lecithin and sphingomyelin in amniotic fluid.

scholarly journals Application Enzymatic Method for Analysis Vaginal Tabletas “Fluomizin”

2021 ◽  
Vol 62 (3) ◽  
pp. 260-269
Author(s):  
Koval'ska Olena Vasilivna ◽  
Blazheyevskіy Mykola
Keyword(s):  
Hydrogen Peroxide ◽  
Enzymatic Reaction ◽  
Chloride Content ◽  
Solution Concentration ◽  
Photometric Method ◽  
Maximal Velocity ◽  
Buffer Solution ◽  
Dequalinium Chloride ◽  
Hydrolysis Of

Introduction: Development of a new enzymatic kinetic-photometric method for analysis of Dequalinium chloride, based on the use of enzymatic hydrolysis of acetylcholine, for determine the amount of Dequalinium chloride in the vaginal tablets “Fluomizin” No 6. Method: The amount of Dequalinium chloride (DCh) was determined by the degree of inhibition of the enzymatic reaction, which was evaluated by the residual unreacted substrate - acetylcholine. Determination of the residual amount of acetylcholine in the reaction mixture was performed by a kinetic-photometric method using an indicator oxidation reaction of p-phenetidine with peracetic acid, which is formed during the auxiliary reaction of perhydrolysis with addition of excess hydrogen peroxide in the reaction mixture over a period of time. Results: Optimal conditions were determined: pH 8.35 was selected, influence of nature of buffer solution, concentration of acetylcholine (0.05 mg / ml), cholinesterase (0.4 mg / ml), hydrogen peroxide (10,0%) and p-phenethedine (1 %), the incubation time (10 min). Conclusions: The procedure for determination of Dequalinium chloride content in the vaginal tablets “Fluomizin” No 6 was developed. The kinetic parameters Km (Michaelis–Menten constant) and Vmax (maximal velocity) were determined.

Reactions in Activated Peroxide Systems and their Influences on Bleaching Performance

2020 ◽  
Vol 17 ◽  
Author(s):  
Xiaoyan Wang ◽  
Jinmei Du ◽  
Changhai Xu
Keyword(s):  
Aqueous Solution ◽  
Hydrogen Peroxide ◽  
Energy Efficiency ◽  
Textile Industry ◽  
High Energy ◽  
Side Reactions ◽  
Competitive Reactions ◽  
High Energy Efficiency ◽  
Hydrolysis Of ◽  
Bleach Activators

Abstract:: Activated peroxide systems are formed by adding so-called bleach activators to aqueous solution of hydrogen peroxide, developed in the seventies of the last century for use in domestic laundry for their high energy efficiency and introduced at the beginning of the 21st century to the textile industry as an approach toward overcoming the extensive energy consumption in bleaching. In activated peroxide systems, bleach activators undergo perhydrolysis to generate more kinetically active peracids that enable bleaching under milder conditions while hydrolysis of bleach activators and decomposition of peracids may occur as side reactions to weaken the bleaching efficiency. This mini-review aims to summarize these competitive reactions in activated peroxide systems and their influence on bleaching performance.

Enzymic colorimetric determination of phosphatidylglycerol in amniotic fluid.

1984 ◽  
Vol 30 (4) ◽  
pp. 534-537 ◽  
Author(s):  
J D Artiss ◽  
M W McGowan ◽  
D R Strandbergh ◽  
E Epstein ◽  
B Zak
Keyword(s):  
Amniotic Fluid ◽  
Fetal Lung ◽  
Aqueous Sample ◽  
Colorimetric Determination ◽  
Glycerol Phosphate ◽  
Ionic Detergent ◽  
Catalyzed Reactions ◽  
Enzyme Catalyzed Reactions ◽  
Hydrolysis Of

Abstract We describe a procedure for the enzymic, colorimetric determination of phosphatidylglycerol in amniotic fluid. After extraction into chloroform:methanol (2:1 by vol) and evaporation, the phospholipid-containing residue is redissolved in a non-ionic detergent, which thus provides an aqueous sample. The subsequent enzymic reaction sequence involves phospholipase-catalyzed hydrolysis of glycerol from its phospholipid. Subsequent enzyme-catalyzed reactions phosphorylate this glycerol and oxidize the resulting glycerol phosphate to produce hydrogen peroxide, which is reacted to produce an intense red chromogen in the peroxidase-catalyzed coupling of 4-aminoantipyrine and 2-hydroxy-3,5-dichlorobenzenesulfonate. When used in conjunction with previously reported enzymic techniques for determination of lecithin and sphingomyelin, this procedure may provide an accurate and precise "lung profile" for assessment of fetal lung maturity.

Dry film for the enzymic determination of total cholesterol in serum.

1982 ◽  
Vol 28 (5) ◽  
pp. 1159-1162 ◽  
Author(s):  
G M Dappen ◽  
P E Cumbo ◽  
C T Goodhue ◽  
S Y Lynn ◽  
C C Morganson ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Cholesterol Oxidase ◽  
Comparison Method ◽  
Total Serum ◽  
Total Serum Cholesterol ◽  
Gelatin Layer ◽  
Control Fluid ◽  
Hydrolysis Of ◽  
Dry Film

Abstract We have prepared a dry film for the enzymic determination of total serum cholesterol. It consists of a transparent support bearing a buffered gelatin layer, and a white reflective spreading layer that contains all of the necessary components for the detection of cholesterol. The method is based on (a) hydrolysis of cholesterol esters to cholesterol by cholesterol ester hydrolase (EC 3.1.1.13), (b) oxidation of cholesterol to cholest-4-en-4-one and hydrogen peroxide by cholesterol oxidase (EC 1.1.3.6), and (c) oxidation of a triarylimidazole leuco dye with hydrogen peroxide in the presence of peroxidase (EC 1.11.1.7) to produce a dye with maximum absorption at about 650 nm. For use over a wider range of concentration, the dye density is read at 540 nm. With reflection densitometry and appropriate mathematical transformation, readings and cholesterol concentrations are linearly related to 5500 mg/L. Results correlate well with those by the Abell-Kendall comparison method (slope 0.97, intercept 92.5, correlation coefficient 0.974, Sy.x = 250.7), and the method is precise (CV of 1.2-2.3% for a control fluid and patients' samples) and relatively free of interferences.

Determination of Carbaryl Residues in Honey Bees

1965 ◽  
Vol 48 (4) ◽  
pp. 771-774
Author(s):  
D P Johnson ◽  
H A Stansbury
Keyword(s):  
Aqueous Solution ◽  
Acetic Acid ◽  
Quantitative Determination ◽  
Honey Bees ◽  
Methylene Chloride ◽  
Hydrolysis Product ◽  
Separate Analysis ◽  
Yellow Substance ◽  
Hydrolysis Of

Abstract A method has been developed for detecting residues of carbaryl (1-naphthyl methylcarbamate) as well as its hydrolysis product, 1-naphthol, in dead bees. The method is based on extraction of the bees with benzene, followed by a cleanup involving liquid partitioning and chromatography on Florisil. The quantitative determination involves hydrolysis of carbaryl to 1-naphthol and coupling of the latter with p-nitrobenzenediazonium fluoborate in acetic acid to form a yellow substance. For separate analysis, free 1-naphthol is separated from methylene chloride into a basic aqueous solution. The sensitivity of the method is about 0.1 ppm; recoveries averaged 85.6 ± 6.6% for 1- naphthol and 83.8 ± 2.7% for carbaryl.

Automated Enzymatic Determination of L-Lactate in Serum, with Use of a Miniature Centrifugal Anlyzer

1976 ◽  
Vol 22 (12) ◽  
pp. 2038-2041 ◽  
Author(s):  
T P Hadjiioannou ◽  
S I Hadjiioannou ◽  
S D Brunk ◽  
H V Malmstadt
Keyword(s):  
Lactate Dehydrogenase ◽  
Reaction Rate ◽  
Enzymatic Reaction ◽  
Reaction Rates ◽  
Enzymatic Determination ◽  
Analytical Recovery ◽  
Rate Method ◽  
Relative Errors ◽  
Lithium Lactate

Abstract We describe an automated enzymatic reaction-rate method for spectrophotometric determination of lactate in serum with a miniature centrifugal analyzer. The L(+)-lactate is selectively oxidized in the presence of lactate dehydrogenase (EC 1.1.1.27) and NAD+ to from NADH, whitch is measured from its absorption. Reaction rates are determined automatically, and unknown concentrations are calculated from a computer0generated calibration curve with aqueous lithium lactate standards. Lactte concentrations in the range 0.32-1.6 µg/4 µl (80-400 mg/liter) of sample were determined with relative errors and coefficient of variation of 4.8%. Analytical recovery of lactate added to pooled serum was 89-112% (average, 101%). Comparison with a kit ("Rapid Lactate") method gave a correlation coefficient squared of 0.979 over a concentration range of 39-779 mg/liter.

The Automated Determination of Serum Uric Acid

1966 ◽  
Vol 12 (11) ◽  
pp. 748-766 ◽  
Author(s):  
Stanley Morgenstern ◽  
Richard V Flor ◽  
James H Kaufman ◽  
Bernard Klein
Keyword(s):  
Uric Acid ◽  
Serum Uric Acid ◽  
Enzymatic Reaction ◽  
Enzymatic Determination ◽  
Before And After ◽  
The Difference ◽  
Automated Determination ◽  
Colorimetric Reaction ◽  
Good Agreement

Abstract An automated procedure is presented for the enzymatic determination of serum uric acid on both the AutoAnalyzer and the Robot Chemist. The procedure measures as the neocuproine complex, the difference in the amount of Cu+ formed by reaction of a Cu++-alkanolamine buffered solution with serum uric acid under precisely controlled conditions before and after uricase treatment of the serum. The difference is proportional to the true serum uric acid content. The elements contributing to the enzymatic reaction, the colorimetric reaction, and the elimination of interferences were investigated. Comparison of serum uric acid values obtained by this method with those obtained by ultraviolet spectrophotometry show very good agreement.

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