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.

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.

Extraction Spectrophotometric Determination of [(2-Chlorophenyl)methylene]propane Dinitrile with Reactive Dyes of the Stabilized Diazonium Salt Type

1992 ◽  
Vol 57 (6) ◽  
pp. 1221-1229
Author(s):  
Emil Halámek ◽  
Zbyněk Kobliha
Keyword(s):  
Mass Spectrometry ◽  
Spectrophotometric Method ◽  
Azo Dye ◽  
Diazonium Salt ◽  
Reactive Dyes ◽  
Diazonium Salts ◽  
Fast Red ◽  
Hydrolysis Of ◽  
C Nmr

A spectrophotometric method has been developed for the determination of [(2-chlorophenyl)methylene]propane dinitrile (CS) stabilized by the diazonium salts Fast Red TR and Fast Blue B after extraction with chloroform. Mass spectrometry, 1H and 13C NMR and elemental analysis confirmed the presence of the hydrazoform of the azo dye formed by reaction with malononitrile, as a product of the alkaline hydrolysis of substance CS, and the diazonium salt Fast Red TR.

Evaluation of a New System for the Kinetic Measurement of Serum Glutamic Oxalacetic Transaminase

1969 ◽  
Vol 15 (6) ◽  
pp. 496-504 ◽  
Author(s):  
Seymour Winsten ◽  
J Henry Wilkinson ◽  
Joseph H Boutwell
Keyword(s):  
Spectrophotometric Method ◽  
New Method ◽  
Activity Levels ◽  
Good Reproducibility ◽  
Kinetic Measurement ◽  
Glutamic Oxalacetic Transaminase ◽  
Serum Glutamic Oxalacetic Transaminase ◽  
New System

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.

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.

Serum Glutamic Oxalacetic Transaminase Assay Using the Sequential Multiple Analyzer (SMA 12/30)

1969 ◽  
Vol 15 (8) ◽  
pp. 730-736 ◽  
Author(s):  
John J Moore ◽  
Sylvan M Sax
Keyword(s):  
Spectrophotometric Method ◽  
Serum Samples ◽  
Glutamic Oxalacetic Transaminase ◽  
Serum Glutamic Oxalacetic Transaminase

Abstract The SMA-12/30 method for serum glutamic oxalacetic transaminase assay gives higher values than are obtained with a reference spectrophotometric method for some serums. A modification of the manifold is made to permit the running of serum blanks. Blank corrections on 466 serum samples indicate that dialysis does not eliminate the need for the blank determination. Acetoacetate interferes in the SMA-12/30 method. The possibility of other interfering substances has not been ruled out.

Colorimetric Determination of Certain Phenol Derivatives in Pharmaceutical Preparations

1981 ◽  
Vol 64 (6) ◽  
pp. 1442-1445
Author(s):  
Sayed M Hassan ◽  
Mohammed I Walash ◽  
Sanaa M El-Sayed ◽  
Abdel Malek Abou Ouf
Keyword(s):  
Pharmaceutical Preparations ◽  
Sulfanilic Acid ◽  
Diazonium Salts ◽  
Colorimetric Determination ◽  
Reaction Products ◽  
Optimum Conditions ◽  
Phenol Derivatives ◽  
The Mean ◽  
Colorimetric Methods

Abstract Simple colorimetric methods are reported for determining both acetaminophen and oxyphenbutazone. These methods are based on coupling between the phenolic compound and the diazonium salts of both sulfanilic acid and p-nitroaniline; the optimum conditions for the reactions were carefully studied. For acetaminophen, the reaction products with diazosulfanilic acid and diazo-p-nitroaniline show maximum absorbance at 480 and 425 nm, respectively. The mean percentage recoveries for authentic samples were 99.5 ± 1.1 and 100.6 ± 0.66, respectively (P = 0.05). For oxyphenbutazone, the obtained colors showed maxima at 385 nm with diazosulfanilic acid and 490 nm with diazo-p-nitroaniline reactions. The mean percentage recoveries for authentic samples were 99.8 ± 0.27 and 100.1 ± 0.57, respectively (P = 0.05). The proposed methods were successfully applied to the analysis of commercial preparations; results were statistically compared with those of other methods.

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