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

1965 ◽  
Vol 11 (1) ◽  
pp. 23-28 ◽  
Author(s):  
Masaki Furuno ◽  
Albert Sheena

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.

1966 ◽  
Vol 12 (4) ◽  
pp. 217-225 ◽  
Author(s):  
J S Annino

Abstract Study of the colorimetric transaminase method of Reitman and Frankel for the determination of serum glutamic oxalacetic transaminase activity revealed the following: (1) although maximum absorption occurs at 444 mµ, absorbance readings at 505 mµ gave satisfactory results; (2) color development is immediate and the color is stable for at least 1 hr.; (3) a pyruvate calibration standard may be used; (4) sample blanks are not usually necessary; (5) a reagent blank should accompany each group of analyses and should be used as a photometric reference; (6) the relationship between dilution and enzyme activity is linear; and (7) although the relationship between incubation time and activity is not exactly linear, a factor has been determined to permit the use of a 12-min. incubation period with samples showing high enzyme activity.


1979 ◽  
Vol 25 (6) ◽  
pp. 860-862 ◽  
Author(s):  
E P Halpern ◽  
R W Bordens

Abstract We describe the application of the microencapsulated-antibody technique to the radioimmunoassay of digoxin in serum. Droplets of emulsified rabbit antibody are microencapsulated in a semipermeable nylon membrane by an interfacial polymerization technique. The antibody microcapsules are incubated with 125I-labeled digoxin and unlabeled digoxin for 15 min at 37 degrees C, then free and bound digoxin are separated by centrifugation. Subtherapeutic, therapeutic, and toxic concentrations of digoxin in sera can be determined, with use of a standard curve prepared by use of known amounts of digoxin. With this technique we obtained an intra-laboratory correlation coefficient of 0.945 for 100 patients' sera and one of 0.940 for interlaboratory results for 21 sera (10 laboratories) when compared to a routine clinical laboratory radioimmunoassay for digoxin. Icterus, lipemia, hemoglobin, or disproteinemia had no effect on the analytical recovery of digoxin. The standard curve was linear to 6 microgram/L; the sensitivity was 0.25 microgram/L.


1997 ◽  
Vol 43 (3) ◽  
pp. 511-517 ◽  
Author(s):  
Gabriele Halwachs-Baumann ◽  
Susanne Katzensteiner ◽  
Wolfgang Schnedl ◽  
Peter Pürstner ◽  
Thomas Pieber ◽  
...  

Abstract We evaluated three newly introduced systems for automated determinations of hemoglobin (Hb) A1c, which allow the processing of large amounts of samples in a routine clinical laboratory. We compared these methods—the Variant HPLC, the Hi-Auto A1c analyzer system, and the Roche immunoassay—with the Diamat HPLC system. All showed good precision and good concordance with the Diamat HPLC. The reference range for Hb A1c has to be determined by the laboratory for each assay system. Interference study showed no statistically significant influence of anemia, polycythemia, rheumatoid factor, or chronic hemodialysis, although individual Hb A1c values can be influenced by polycythemia (when measured with the Hi-Auto A1c analyzer) and by chronic hemodialysis (when measured with the Variant HPLC). HPLC was not suitable for measuring Hb A1c in the examined cases of hemoglobin variants; assaying fructosamine seems to be better for monitoring these patients.


1979 ◽  
Vol 25 (2) ◽  
pp. 285-288 ◽  
Author(s):  
P V Sundaram ◽  
W Hinsch

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.


1967 ◽  
Vol 13 (3) ◽  
pp. 175-185 ◽  
Author(s):  
Sylvan M Sax ◽  
John J Moore

Abstract A method for measuring serum glutamic oxalacetic transaminase activity is described, in which substrate concentrations are more nearly optimal than in previous colorimetric methods. By coupling the diazonium salt at a pH of 4.2, interference from α-oxoglutarate is negligible. Oxalacetate is produced at a linear rate to 180 I.U. Results correlate well with those obtained by a reference spectrophotometric method.


1971 ◽  
Vol 17 (12) ◽  
pp. 1200-1201 ◽  
Author(s):  
Wesley A Dill ◽  
Lucy Chucot ◽  
Tsun Chang ◽  
Anthony J Glazko

Abstract Diphenylhydantoin (DPH) is extracted from plasma with ethylene dichloride, returned to alkali, and oxidized with permanganate in glass-stoppered test tubes containing a layer of iso-octane. The absorbance of the oxidation product (benzophenone) in the iso-octane layer is measured spectrophotometrically. This procedure eliminates interference by chloroform that is encountered in other methods; highly specialized reflux condensers or distillation equipment is not needed; and the cost of solvents is decreased. The procedure is highly specific; it detects less than 1 µg of DPH per milliliter of plasma, and it is suitable for routine clinical laboratory use.


1969 ◽  
Vol 15 (6) ◽  
pp. 496-504 ◽  
Author(s):  
Seymour Winsten ◽  
J Henry Wilkinson ◽  
Joseph H Boutwell

Abstract A new spectrophotometric method for the determination of serum glutamic oxalacetic transaminase§ (SGOT) is described which uses standardized technics and prepackaged reagents. A study was made of this new method in three laboratories and was compared with the routine methods, using identical serum specimens. The new procedure gave good reproducibility and precision. In all methods studied there was evidence of failure of linearity of response at the two highest activity levels examined.


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