Journal of The Showa Medical Association
Online ISSN : 2185-0976
Print ISSN : 0037-4342
ISSN-L : 0037-4342
STUDY OF L-GLUTAMATE DEHYDROGENASE (GLDH) ESPECIALIY, ON METHOD FOR ASSAY, ENZYMIC SOURCE, RANGE OF NORMAL VALUE AND CLINICAL SIGNIFICANCE
Kunihide Gomi
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1973 Volume 33 Issue 4 Pages 489-497

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Abstract
GLDH activity in rabbit liver was measured spectrophotometrically using reduced nicotineamide adenine dinucleotide (NADH) oxidation reaction. Optimum condition for mea-surement was obtained in a reaction mixture of 1/10 M of phosphate buffer (pH 8.6), 1/8 M of α-ketoglutarate and 2 M NH4Cl.
Rabbit was used as a experimental animal thoughout. In liver the highest GLDH activity was obtained, while lower activities were found in kidney, lung, small intestine and skeletal muscle.
The GLDH was mainly located in mitocondrial fraction. A small amount of GLDH activity was found in nuclear fraction and almost no activity was found in supernatant fraction.
When it was kept in freezer (-20°C) for 24 hrs., 15% of GLDH activity was lost and then it was stable for a week.
In sera of normal 15 Japanese blood donors, mean of GLDH activity was 0.56 mU/ml (0-1.2 mU/ml) .
In cases of hepatitis, higher GLDH activity, while in cases of the other disease no change were observed. In rabbits with acute toxic hepatitis induced by carbon tetrahydro-chloride, higher activity was obtained in the early stages and the changes of value of GLDH were paralleled with that of GOT and not paralleled with that of LDH.
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