Colorimetric determination of serum glutamic-oxalacetic transaminase activity

1968 ◽  
Vol 20 (1) ◽  
pp. 165-166 ◽  
Author(s):  
Peter J. Healy
Keyword(s):  
Colorimetric Determination ◽  
Transaminase Activity ◽  
Glutamic Oxalacetic Transaminase ◽  
Serum Glutamic Oxalacetic Transaminase

A Study of the Colorimetric Dinitrophenylhydrazine Method for the Determination of Serum Glutamic Oxalacetic Transaminase Activity

1966 ◽  
Vol 12 (4) ◽  
pp. 217-225 ◽  
Author(s):  
J S Annino
Keyword(s):  
Enzyme Activity ◽  
Transaminase Activity ◽  
Reagent Blank ◽  
Glutamic Oxalacetic Transaminase ◽  
Color Development ◽  
High Enzyme ◽  
Serum Glutamic Oxalacetic Transaminase ◽  
The Relationship ◽  
High Enzyme Activity

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.

Determination of Glutamic Oxalacetic Transaminase Activity by Coupling of Oxalacetate with Diazonium Salts

1967 ◽  
Vol 13 (3) ◽  
pp. 175-185 ◽  
Author(s):  
Sylvan M Sax ◽  
John J Moore
Keyword(s):  
Spectrophotometric Method ◽  
Diazonium Salt ◽  
Diazonium Salts ◽  
Transaminase Activity ◽  
Linear Rate ◽  
Glutamic Oxalacetic Transaminase ◽  
Serum Glutamic Oxalacetic Transaminase ◽  
Substrate Concentrations ◽  
Colorimetric Methods

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.

Improved Method for the Colorimetric Determination of Glutamic-Oxalacetic Transaminase Activity

1957 ◽  
Vol 3 (6) ◽  
pp. 703-710 ◽  
Author(s):  
Fred L Humoller ◽  
Joseph M Holthaus ◽  
John R Walsh
Keyword(s):  
Colorimetric Determination ◽  
Transaminase Activity ◽  
Improved Method ◽  
Glutamic Oxalacetic Transaminase ◽  
Proposed Modification

Abstract A modification of the Cabaud et at. method (1) for the determination of SGOT activity is described. The proposed modification consists of the elimination of the interference of unreacted DNPH by extracting the pyruvate dinitrophenyihydrazone with aqueous bicarbonate. The proposed method also employs a lower concentration of alpha-ketoglutarate, thus reducing its competition for the available DNPH.

Electrophoretic Migration Pattern of Serum Glutamic Oxalacetic Transaminase

1958 ◽  
Vol 4 (1) ◽  
pp. 13-21 ◽  
Author(s):  
Herndon G Shepherd ◽  
Hugh J McDonald
Keyword(s):  
Pyridoxal Phosphate ◽  
Serum Proteins ◽  
Migration Pattern ◽  
Globulin Fraction ◽  
Transaminase Activity ◽  
Rat Serum ◽  
Glutamic Oxalacetic Transaminase ◽  
Electrophoretic Migration ◽  
Serum Glutamic Oxalacetic Transaminase

Abstract Using the combined technics of the ionographic separation of serum proteins in a paper-stabilized medium, as described by McDonald et al. (16, 17, 18), and the spectrophotometric procedure for the determination of transaminase activity developed by Karmen (3, 14), the electrophoretic migration pattern of the enzyme glutamic oxalacetic transaminase in rat serum has been examined. The major portion of the transaminase activity has been found to be associated with the α-2 globulin fraction of the serum proteins. Further evidence has been presented for the assumption of a nonionic linkage between the enzyme and its coenzyme, pyridoxal phosphate.

Sources of Variation in a Standardized and a Semi-micro Procedure for the Spectrophotometric Assay of Serum Glutamic-Oxalacetic Transaminase Concentration

1958 ◽  
Vol 4 (5) ◽  
pp. 392-408 ◽  
Author(s):  
A J Schneider ◽  
Myron J Willis
Keyword(s):  
Arrhenius Equation ◽  
Spectrophotometric Assay ◽  
Light Path ◽  
Transaminase Activity ◽  
Arrhenius Law ◽  
Glutamic Oxalacetic Transaminase ◽  
Sources Of Variation ◽  
The Mean ◽  
Serum Glutamic Oxalacetic Transaminase ◽  
Temperature Factors

Abstract 1. Both a standard method and a semi-micro method for the spectrophotometric assay of serum glutamic-oxalacetic transaminase (S-GOT) concentrations have been described. 2. Either procedure is associated with an error defined by a factor of less than 1.03. 3. The temperature dependence of the rate of transamination was shown to follow Arrhenius' law over the range of temperature from 25° to 38°. 4. A tabulation of temperature factors calculated from the derived Arrhenius equation was presented. These factors permit correction of rates observed at temperature T to rates expected at 32°. 5. A comparison of normal S-GOT values from various sources was made, with correction for temperature differences. Based on 779 values from four different laboratories, the combined mean for adults was 21.9. 6. A standard unit of transaminase activity was defined and referred to as a Karmen unit. A Karmen unit represents that amount of transaminase in 1 ml. of sample which will cause a decrease in optical density at 340 mµ of 0.001 per minute at a temperature of 32°, an effective light path of 1 cm., and a volume of test solution of 3 ml. According to this definition, the mean normal adult S-GOT concentration is 21.9 Karmen units. The practical upper limit of normal will be defined in another publication.

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
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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