Single- and coupled-enzyme nylon tube reactors for routine determination of pyruvate and lactate in serum.

Abstract We describe the use of a continuous-flow clinical analyzer with an immobilized coupled-enzyme nylon tube reactor and an immobilized single-enzyme nylon tube reactor for routine estimation of lactate and pyruvate in serum. These reactors are incorporated into the flow system of a modified continuous-flow analyzer (Technicon AutoAnalyzer). Results for serum lactate and pyruvate by this method are compared with those by corresponding methods in which the same enzymes are used in solution, either automatically (pyruvate) or manually (lactate) performed. Routine clinical laboratory determinations with use of the coupled-enzyme system lactate dehydrogenase and alanine aminotransferase, co-immobilized in the nylon tube reactor for estimation of lactate, and lactate dehydrogenase reactors for estimation of pyruvate give reliable and reproducible results with high precision at low cost.

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Single- and coupled-enzyme nylon-tube reactors for plasma glucose determination with glucose oxidase and aldehyde dehydrogenase.

Clinical Chemistry ◽

10.1093/clinchem/26.12.1652 ◽

1980 ◽

Vol 26 (12) ◽

pp. 1652-1655 ◽

Cited By ~ 8

Author(s):

W Hinsch ◽

A Antonijewić ◽

P V Sundaram

Keyword(s):

Glucose Oxidase ◽

Aldehyde Dehydrogenase ◽

Plasma Glucose ◽

Continuous Flow ◽

Flow System ◽

Low Cost ◽

Immobilized Enzymes ◽

Glucose Determination ◽

Nylon Tube

Abstract We describe routine methods for determining glucose in plasma with use of aldehyde dehydrogenase or glucose oxidase-aldehyde dehydrogenase immobilized in a nylon tube that is integrated into a continuous-flow system. Although the coupled-enzyme nylon-tube reactors require the presence of a third enzyme, catalase, in solution, the kinetics are not so complicated as to preclude reliable routine determination of glucose at very low cost. Precision is good, and results correlate well with those by the method involving glucose oxidase in solution. More than 3000 tests may be carried out with one reactor. The immobilized enzymes are stable for several months at 4 degrees C when not in use.

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Immobilized-enzyme nylon-tube reactors for routine determination of urea and citrulline in serum.

Clinical Chemistry ◽

10.1093/clinchem/24.2.234 ◽

1978 ◽

Vol 24 (2) ◽

pp. 234-239 ◽

Cited By ~ 16

Author(s):

P V Sundaram ◽

M P Igloi ◽

R Wassermann ◽

W Hinsch ◽

K J Knoke

Keyword(s):

Solution Method ◽

Immobilized Enzyme ◽

Low Cost ◽

System A ◽

Tube Reactor ◽

Nylon Tube ◽

Diacetyl Monoxime ◽

Flow Through ◽

Continued Use

Abstract A continuous-flow clinical analyzer for the routine estimation of urea is described that makes use of an immobilized-enzyme nylon-tube reactor as part of a flow-through system (a Technicon AutoAnalyzer I). Results of blood-urea analyses by use of the immobilized urease are compared with determinations made with the diacetyl monoxime method and the urease solution method. Clinical trials carried out routinely with the immobilized enzyme nylon tube reactor give reliable and reproducible results with high precision and low cost. The reactors are stable to intermittent or continued use for at least four months or for 2000 tests. A method is described in which differential colorimetry is used for determining citrulline in blood and which makes use of the immobilized urease, albeit indirectly.

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A Rapid Electrophoretic Method for the Determination of the Isoenzymes of Serum Lactate Dehydrogenase

Clinical Chemistry ◽

10.1093/clinchem/12.5.308 ◽

1966 ◽

Vol 12 (5) ◽

pp. 308-313 ◽

Cited By ~ 8

Author(s):

Albert W Opher ◽

Charles S Collier ◽

Joseph M Miller

Keyword(s):

Enzyme Activity ◽

Lactate Dehydrogenase ◽

Quantitative Determination ◽

Serum Lactate ◽

Serum Lactate Dehydrogenase ◽

Electrophoretic Method ◽

The Individual ◽

Electrophoretic Procedure ◽

Purple Formazan

Abstract A convenient electrophoretic procedure for the separation and quantitation of lactate dehydrogenase (LDH) isoenzymes is described. The system uses polyacetate Sepraphore III strips.* The areas of activity are shown by incubation with an LDH substrate combined with tetra-nitro-blue-tetrazolium. The reduction of the latter to the purple formazan is quantitatively related to the enzyme activity. Quantitative determination of the individual colored areas is performed by densitometry.

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Automated enzymic determination of glycerol in beverages by an immobilized glycerol dehydrogenase nylon-tube reactor

European Food Research and Technology ◽

10.1007/bf01907238 ◽

1980 ◽

Vol 171 (6) ◽

pp. 449-450 ◽

Cited By ~ 4

Author(s):

Wilhelm Hinsch ◽

Andreas Antonijevic ◽

V. Sundaram

Keyword(s):

Glycerol Dehydrogenase ◽

Tube Reactor ◽

Nylon Tube

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Adaptation of Babson's Method for the Determination of Serum Glutamic Oxalacetic Transaminase in the Clinical Laboratory

Clinical Chemistry ◽

10.1093/clinchem/11.1.23 ◽

1965 ◽

Vol 11 (1) ◽

pp. 23-28 ◽

Cited By ~ 6

Author(s):

Masaki Furuno ◽

Albert Sheena

Keyword(s):

Clinical Laboratory ◽

Glutamic Oxalacetic Transaminase ◽

Laboratory Workers ◽

Routine Clinical Laboratory ◽

Serum Glutamic Oxalacetic Transaminase ◽

Final Color

Abstract Babson's method for the assay of serum glutamic oxalacetic transaminase (SGO-T) is modified to increase its accuracy and reliability. The final color produced is made stable with the addition of bisulfite ion, thereby making the procedure more suitable for the routine clinical laboratory. The 95% limits for values on 20 healthy laboratory workers was 4 to 26 units with a mean of 13 units.

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The Automated Determination of NAD-Coupled Enzymes

Clinical Chemistry ◽

10.1093/clinchem/12.5.274 ◽

1966 ◽

Vol 12 (5) ◽

pp. 274-281 ◽

Cited By ~ 11

Author(s):

Stanley Morgenstern ◽

Richard Flor ◽

Gerald Kessler, ◽

Bernard Klein

Keyword(s):

Lactate Dehydrogenase ◽

Excellent Agreement ◽

Nicotinamide Adenine Dinucleotide ◽

Colorimetric Method ◽

Serum Lactate ◽

Serum Lactate Dehydrogenase ◽

Coupled Enzymes ◽

Reduced Nicotinamide Adenine Dinucleotide ◽

Automated Determination

Abstract A precise automated procedure developed for determination of serum lactate dehydrogenase, using the Robot Chemist, measures absorbance of a cuprous-neo-cuproine complex formed by coupled reduction of the cupric-neocuproine reagent with enzymatically generated reduced nicotinamide adenine dinucleotide. Activity values obtained by this method, by the identical automated colorimetric method on the AutoAnalyzer, and by an automated spectrophotometric (34O-mµ) procedure show excellent agreement.

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Pyruvate as Substrate in the Determination of Serum Lactate Dehydrogenase Isoenzyme Activity

Clinical Chemistry ◽

10.1093/clinchem/20.11.1462 ◽

1974 ◽

Vol 20 (11) ◽

pp. 1462-1465 ◽

Cited By ~ 1

Author(s):

Doris McKenzie ◽

A R Henderson

Keyword(s):

Lactate Dehydrogenase ◽

Serum Lactate ◽

Serum Lactate Dehydrogenase ◽

Dehydrogenase Isoenzyme

Abstract Lactate dehydrogenase isoenzyme activity is usually assessed, after the isoenzymes have been separated, by reactions involving lactate as the substrate. We describe a method for their assessment with pyruvate as the substrate. Precision is adequate as compared to the conventional methodology. Application of this type of approach (measurement of a decrease in fluorescence) to determination of other serum isoenzymes is briefly described.

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Improvements in and clinical utility of a continuous-flow method for routine measurement of dialyzable (ultrafiltrable) calcium.

Clinical Chemistry ◽

10.1093/clinchem/25.11.1939 ◽

1979 ◽

Vol 25 (11) ◽

pp. 1939-1943 ◽

Cited By ~ 6

Author(s):

J Toffaletti ◽

G N Bowers

Keyword(s):

Continuous Flow ◽

Clinical Utility ◽

Clinical Laboratory ◽

Serum Samples ◽

The Past ◽

Baseline Noise ◽

Routine Service ◽

Routine Measurement ◽

Routine Clinical Laboratory ◽

Continuous Flow Method

Abstract We describe modifications to the original continuous-flow procedure for dialyzable calcium (Clin. Chem. 23: 1258, 1977) needed to make the method more suitable for routine clinical laboratory use. The modifications simplify the continuous-flow (AutoAnalyzer) manifold, decrease baseline noise, increase the sensitivity, and permit use of a less-expensive fluorometer. Bias due to variation in serum processing is minimized by use of serum samples minimally exposed to air and a pH 7.40 buffer in place of the routinely processed sera and pH 7.30 buffer used formerly. Day-to-day precision (CV) during the past year for samples that included three different lots of quality-control sera was 2 to 3%. The analysis requires 200 micro L of serum, collected with minor additional precautions. We find that dialyzable calcium can be dependably measured in the routine service laboratory and show how this information is clinically more useful than is information on total calcium in serum.

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Automation of Interpretive Clinical Laboratory Reports: Isoenzymes of Serum Lactate Dehydrogenase

Laboratory Medicine ◽

10.1093/labmed/10.10.636 ◽

1979 ◽

Vol 10 (10) ◽

pp. 636-639 ◽

Cited By ~ 1

Author(s):

David S. Jacobs ◽

Gary M. Clark ◽

Alvin L. Beers ◽

Gary Palmer

Keyword(s):

Lactate Dehydrogenase ◽

Clinical Laboratory ◽

Serum Lactate ◽

Serum Lactate Dehydrogenase

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The effect of respiratory diseases on serum lactate dehydrogenase and its isoenzyme patterns in calves

Polish Journal of Veterinary Sciences ◽

10.2478/pjvs-2013-0030 ◽

2013 ◽

Vol 16 (2) ◽

pp. 211-218 ◽

Cited By ~ 4

Author(s):

O. Nagy ◽

Cs. Tóthová ◽

I. Paulíková ◽

G. Kováčl ◽

H. Seidel

Keyword(s):

Lactate Dehydrogenase ◽

Respiratory Diseases ◽

Clinical Signs ◽

Serum Lactate ◽

Serum Lactate Dehydrogenase ◽

Control Group ◽

Diagnostic Significance ◽

Organ Systems ◽

Isoenzyme Patterns

AbstractIn this study we examined the serum activity of lactate dehydrogenase (LDH) and its isoenzyme patterns in 28 calves of a lowland black spotted breed and its crossbreeds at the age of 2-6 months suffering from clinically noticeable manifested respiratory diseases - bronchopneumonia (BRD Group). As a control group we used 35 clinically healthy calves of the same age, breed and nutrition (Healthy Group). The sick calves did not show clinical signs or pathological lesions on other organ systems. The results found in sick calves showed a significantly higher total activity of LDH than in clinically healthy animals (P<0.01). The mean activity of LDH was 2012 U/l in healthy calves and in calves with respiratory diseases 2529 U/l. The differences in all LDH isoenzyme patterns between both groups of animals were significant (P<0.001) and in calves with respiratory diseases are characterized by a marked increase of the LDH 1 fraction and a decrease in the proportion of the other four LDH isoenzymes. Our results differ from those observed and presented in respiratory diseases in human medicine or in sheep. The explanation for the obtained results in calves and the determination of their diagnostic significance needs further studies and investigations using more animals with various severity of clinical signs and pathological changes, including analysis and determination of lactate dehydrogenase isoenzyme patterns in healthy and affected cattle lung tissue.

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