Determination of Glucose in Biologic Fluids with an Automated Enzymatic Procedure

1965 ◽  
Vol 11 (9) ◽  
pp. 840-845 ◽  
Author(s):  
Michael Robin ◽  
Abraham Saifer
Keyword(s):  
Glucose Oxidase ◽  
Acid Concentration ◽  
Sampling Rate ◽  
Good Reproducibility ◽  
Normal Range ◽  
High Acid Concentration ◽  
Threefold Increase ◽  
Enzymatic Determination ◽  
Enzymatic Procedure

Abstract An automated procedure for the enzymatic determination of "true" glucose with the glucose oxidase-peroxidase system is described. A threefold increase in sensitivity was obtained through measurement of the stable, pink chromogen obtained at high acid concentration. Good reproducibility and stoichiometry was obtained over the range of 50-400 mg./l00 ml. at a sampling rate of 40/hr. The normal range (70-105 mg./100 ml.) and the error of the method (±2.0%) are about the same as that obtained with the manual method of Saifer and Gerstenfeld (7).

Determination of Glucose by an Improved Enzymatic Procedure

1961 ◽  
Vol 7 (5) ◽  
pp. 542-545 ◽  
Author(s):  
Mary E Washko ◽  
Eugene W Rice
Keyword(s):  
Sulfuric Acid ◽  
Glucose Oxidase ◽  
Phosphate Buffer ◽  
Sulfuric Acid Concentration ◽  
Buffering Capacity ◽  
Enzymatic Determination ◽  
Colored Product ◽  
The Stability ◽  
Enzymatic Procedure

Abstract The glucose oxidase-peroxidase system for the enzymatic determination of glucose was investigated with respect to the instability of the enzyme reagent, the buffering capacity of the reaction milieu, and the stability and sensitivity of the final chromogen. An improved procedure was developed in which the enzyme solution is both stabilized and more adequately buffered by reconstitution in 40% aqueous glycerol containing 0.04 M phosphate buffer, pH 7.0. The sensitivity and stability of the colored product is markedly increased when a final sulfuric acid concentration of 4.9 N is used.

An Automated, Saccharogenic Method for Determining Serum Amylase Activity

1970 ◽  
Vol 16 (12) ◽  
pp. 985-989 ◽  
Author(s):  
Wendell R O'Neal ◽  
Nathan Gochman
Keyword(s):  
Glucose Oxidase ◽  
Blood Donors ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Serum Glucose ◽  
Normal Range ◽  
Reducing Substances ◽  
Serum Amylase Activity

Abstract An automated adaptation of the Somogyi saccharogenic determination of serum amylase is described in which conventional AutoAnalyzer modules are used. Adequate sensitivity with short incubation is achieved by incorporating glucose oxidase and catalase in the substrate to destroy serum glucose during incubation. Maltose and other dialyzable oligosaccharides are measured with the alkaline copper-neocuproine reaction. A simultaneous blank run is performed to determine reducing substances other than glucose in serum. Precision studies and correlation with a manual saccharogenic method are presented. The normal range was determined from data for 49 healthy blood donors.

Enzymatic determination of serum 12α-hydroxy bile acid concentration with 12α-hydroxysteroid dehydrogenase

1988 ◽  
Vol 23 (6) ◽  
pp. 646-651 ◽  
Author(s):  
Naoki Tamasawa ◽  
Masashi Yoneda ◽  
Isao Makino ◽  
Kazuo Takebe ◽  
Shigeru Ueda ◽  
...  
Keyword(s):  
Bile Acid ◽  
Acid Concentration ◽  
Hydroxysteroid Dehydrogenase ◽  
Bile Acid Concentration ◽  
Enzymatic Determination

Enzymatic Determination of Starch in Feeds, Feed Ingredients, and Feces

1969 ◽  
Vol 52 (5) ◽  
pp. 956-958
Author(s):  
W W Turner
Keyword(s):  
Glucose Oxidase ◽  
Constant Temperature ◽  
Enzyme System ◽  
Aqueous Alcohol ◽  
Feed Ingredients ◽  
Enzymatic Determination ◽  
Oxidase Enzyme

Abstract Starch is determined in various materials such as feeds, grains, cereals, grasses, and feces by the combination of some existing techniques plus new methodology. Samples are extracted with aqueous alcohol and hydrolyzed with HCl; the resulting glucose is measured with a glucose oxidase enzyme system. The actual handling operations, including troublesome nitrations and constant temperature baths, are minimized or eliminated.

Optimal Conditions for the Enzymatic Determination of L-Lactic Acid

1962 ◽  
Vol 8 (1) ◽  
pp. 1-10 ◽  
Author(s):  
G F Olson
Keyword(s):  
Lactic Acid ◽  
Heart Muscle ◽  
Lactic Dehydrogenase ◽  
Test System ◽  
Optimal Conditions ◽  
Enzymatic Method ◽  
Chemical Methods ◽  
Enzymatic Determination ◽  
Enzymatic Procedure

Abstract A simple enzymatic method for the determination of lactic acid with muscle lactic dehydrogenase is described. L(+) Lactate in amounts from 0.04 µM to 0.4 µM can be directly measured by following the formation of reduced diphosphopyridine nucleotide at 340 mµ. The effect of varying the concentrations of reactants in the test system was studied, and the optimal concentrations for stoichiometric conversion of lactate to pyruvate were determined. When lactic acid concentrations in plasma, liver, and heart muscle were determined by both enzymatic and chemical methods, identical results were obtained. The advantages of the present enzymatic procedure over chemical methods are discussed.

scholarly journals Multicommuted flow system for the determination of glucose in animal blood serum exploiting enzymatic reaction and chemiluminescence detection

2003 ◽  
Vol 25 (5) ◽  
pp. 109-114 ◽  
Author(s):  
Cherrine K. Pires ◽  
Patrícia B. Martelli ◽  
Boaventura F. Reis ◽  
José L. F. C. Lima ◽  
Maria Lúcia M. F. S. Saraiva
Keyword(s):  
Blood Serum ◽  
Glucose Oxidase ◽  
Confidence Level ◽  
Sampling Rate ◽  
Enzymatic Reaction ◽  
Porous Silica ◽  
Previous Treatment ◽  
Chemiluminescence Detection ◽  
Animal Blood

An automatic flow procedure based on multicommutation dedicated for the determination of glucose in animal blood serum using glucose oxidase with chemiluminescence detection is described. The flow manifold consisted of a set of three-way solenoid valves assembled to implement multicommutation. A microcomputer furnished with an electronic interface and software written in Quick BASIC 4.5 controlled the manifold and performed data acquisition. Glucose oxidase was immobilized on porous silica beads (glass aminopropyl) and packed in a minicolumn (15 } 5 mm). The procedure was based on the enzymatic degradation of glucose, producing hydrogen peroxide, which oxidized luminol in the presence of hexacyanoferrate(III), causing the chemiluminescence. The system was tested by analysing a set of serum animal samples without previous treatment. Results were in agreement with those obtained with the conventional method (LABTEST Kit) at the 95% confidence level. The detection limit and variation coefficient were estimated as 12.0 mg l−1(99.7% confidence level) and 3.5% (n=20), respectively. The sampling rate was about 60 determinations h−1with sample concentrations ranging from 50 to 600 mg l−1glucose. The consumptions of serum sample, hexacyanoferrate(III) and luminol were 46 μl, 10.0 mg and 0.2 mg/determination, respectively.

Fluorimetric–enzymatic determination of glucose based on labelled glucose oxidase

1998 ◽  
Vol 368 (1-2) ◽  
pp. 97-104 ◽  
Author(s):  
Jose F Sierra ◽  
Javier Galban ◽  
S de Marcos ◽  
Juan R Castillo
Keyword(s):  
Glucose Oxidase ◽  
Enzymatic Determination

The Kodak Ektachem 400 Analyzer evaluated for automated enzymic determination of plasma creatinine.

1983 ◽  
Vol 29 (7) ◽  
pp. 1422-1425 ◽  
Author(s):  
C H Smith ◽  
M Landt ◽  
M Steelman ◽  
J H Ladenson
Keyword(s):  
Plasma Creatinine ◽  
Normal Range ◽  
End Point ◽  
Enzymatic Procedure

Abstract We have evaluated an automated creatinine iminohydrolase procedure for plasma creatinine analysis, as used in the Kodak Ektachem 400 Analyzer. The correlation with kinetic and end-point (equilibrium) alkaline picrate procedures is generally excellent. The enzymatic procedure has the advantage of being unaffected by bilirubin, cephalosporins, and acetoacetate, all of which interfere in alkaline picrate procedures. Its accuracy, however, greatly depends on calibration values provided by the manufacturer. Storage of samples at -20 degrees C produced little change in measured creatinine. The Ektachem procedure has a greater range of linearity (140 mg/L) than the alkaline picrate procedures, but it shares with them the disadvantages of suboptimal precision in the normal range. The increased specificity, ease of performance, and other advantages of this use of creatinine iminohydrolase make it an attractive procedure.

Enzymatic determination of D-mannose in serum.

1984 ◽  
Vol 30 (2) ◽  
pp. 293-294 ◽  
Author(s):  
K Soyama
Keyword(s):  
Healthy Volunteers ◽  
Glucose Oxidase ◽  
Fungal Infections ◽  
Enzymatic Assay ◽  
Glucosephosphate Isomerase ◽  
Enzymatic Determination ◽  
Endogenous Glucose ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract A new and simple enzymatic assay for measuring D-mannose in serum is described. Endogenous glucose is eliminated from serum by use of glucose oxidase (EC 1.1.3.4) and catalase (EC 1.11.1.6). D-Mannose concentration is calculated from the increase in NADH formation after mannosephosphate isomerase (EC 5.3.1.8) is added. This increase is a result of coupling the following series of enzymes: hexokinase (EC 2.7.1.1), glucosephosphate isomerase (EC 5.3.1.9), and glucose-6-phosphate dehydrogenase (EC 1.1.1.49, NAD+-dependent). The study included subjects who were healthy volunteers and patients with suspected or proven fungal infections.

Specific Enzymatic Determination of Glucose in Blood and Urine Using Glucose Oxidase

Diabetes ◽  
1956 ◽  
Vol 5 (1) ◽  
pp. 1-6 ◽  
Author(s):  
E. R. Froesch ◽  
A. E. Renold ◽  
B. McWilliams
Keyword(s):  
Glucose Oxidase ◽  
Enzymatic Determination
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