Studies on glutamic pyruvic- and oxaloacetic transaminase of different organs of Ascaris <i>lumbricoides suis</i>

, Chu, Jung Kyun; , Chang, Min Choo

doi:1975.13.1.53

Korean J Parasito > Volume 13(1):1975 > Article

Original Article


Korean J Parasitol. 1975 Jun;13(1):53-59. English. Published online Mar 20, 1994. http://dx.doi.org/10.3347/kjp.1975.13.1.53
Copyright © 1975 by The Korean Society for Parasitology


Studies on glutamic pyruvic- and oxaloacetic transaminase of different organs of Ascaris lumbricoides suis
Jung-Kyun Chu and Min-Choo Chang
Department of Parasitology, School of Medicine, Kyung-Hee University, Korea.



Abstract
A Study on glutamic pyruvic and oxaloacetic transaminase of different organs(e.g intestine, seminal vesicle, reticular tissue, uterus, ovary, testes) in Ascaris lumbricoides suis have been investigated. The activity of transaminase were determined on the whole homogenates and subcellular fractions separated by differential centrifugation. The activity of glutamic pyruvic and oxaloacetic were assayed by colorimetric method of Reitman-Frankel. The results were obtained as follows: 1. About ninty percent of the glutamic pyruvic and oxaloacetic transaminase in different organs was found to be localized in the supernatant fraction with the separation of differential centrifugation. And it was found that ten percent of glutamic pyruvic and oxaloacetic transaminase exists in the mitochondrial fraction. 2. The specific activity of glutamic oxaloacetic transnaminase in different organs was relatively higher than the glutamic pyruvic transaminase activity.

Figures

Fig. 1
Effect of diluted enzyme solution on transaminase activity of the intestne homogenate in Ascaris lumbricoides assayed Reitman-Frankel. The intestine homogenates were diluted as indicated as with 0.25M sucrose-0.05M K₂HPO₄ solution. Incubation mixture consisted of 1ml of 2mM α-Ketoglutarate containing 200mM L-aspartate, 1-alanine and 1ml of 0.1M phosphate buffer(pH 7.4). After preincubation for 5 minutes at 37℃, 5-20µg of diluted enzyme solution as indicated was added. After incubation was made for 30-60 minutes at 37℃, 1ml of 1mM 2,4-dinitrophenylhydrazine was added to the reaction mixture and allowed to stand for 20 minutes at room temperature. Color was developed by adding 10ml of 0.4N NaOH. Optical density of colored compound read at 505nm. One Reitman-Frankel unit is equivalent to one Karmen unit which is defined as the enzyme amount catalyzing the formation of 4.82×10^-4moles of glutamate per minute at pH 7.5 and at 25℃. Optical density changes as calculated by the expression: △gO.D.-blank O.D.

Tables


	Table 1 Subcellular Localization of G.O.T. (Male)


	Table 2 Subcellular Localization of G.P.T. (Male)


	Table 3 Calculation of the Specific Activity in G.O.T. and G.P.T. (Male)


	Table 4 Protein content of each fractions (Male)


	Table 5 Subcellular Localization of G.O.T. (Female)


	Table 6 Subcellular Localization of G.P.T. (Female)


	Table 7 Calculation of the Specific Activity in G.O.T. and G.P.T. (Female)


	Table 8 Protein content of each fractions (Female)


	Table 9 Detemination of G.P.T. and G.O.T. Activity in Body Fluid (Female)

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