• Journal of Radiation Protection and Research
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• v.18 no.2
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• pp.61-69
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• 1993

We examined various enzyme activity changes by intraperitoneal injection uranium in the carp liver. These enzyme activity changes can be used as biochemical indicators of internal exposure to uranium. The results were followings ; 1) Total protein concentration decreased by intraperitoneal injection in the carp liver. 2) Lysosomal acid pretense and ${\beta}-glucuronidase$ activities increased in the liver until sixth intraperitoneal injection of uranium, but Lysosomal acid phosphatase activities decreased in the liver until the sixth injection of uranium. 3) Alkaline phosphatase activities sharply increased and Glutamate oxaloacetate Transaminase activities steadily decreased in the liver until the sixth injection of uranium. 4) Creatine %kinase activities steadily decreased and malate dehydrogenase activities sharply decreased in the liver after the primary injection of uranium. Any malate dehydrogenase activities was not detected after sixth injection of uranium.

• Asian-Australasian Journal of Animal Sciences
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• v.17 no.9
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• pp.1188-1191
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• 2004

Two species of marine catfish, Arius maculatus and Osteogeneiosus militaris, belonging to family Ariidae were analysed electrophoretically for genetic variation in 6 enzymes, alcohol dehydrogenase (ADH), malate dehydrogenase (MDH), lactate dehydrogenase (LDH), glucose dehydrogenase (GDH), malic enzyme (ME) and superoxide dismutase (SOD). Eighteen individuals of each species were studied. Two loci MDH and ADH were polymorphic in both. Average heterozygosity in A. maculatus was 1.46, while it was 2.5 in O. militaris. The allele frequencies were used to estimate Nei's genetic distance (D). The D value was calculated to be 0.6879. Two isozyme loci, ME and SOD, were found to be the most reliable species specific markers. No tissue specific loci were observed for the enzymes studied, the bands being identical in each case. The genetic distance observed between O. militaris and A. maculatus in this study suggests that they would be more appropriately classified as species of the same genus rather than being assigned separate genera.

• Journal of Microbiology and Biotechnology
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• v.20 no.3
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• pp.542-549
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• 2010

In the present study, overexpression, purification, and characterization of Aeropyrum pernix K1 chaperonin B in E. coli were investigated. The chaperonin $\beta$-subunit gene (ApCpnB, 1,665 bp ORF) from the hyperthermophilic archaeon A. pernix K1 was amplified by PCR and subcloned into vector pET21a. The constructed pET21a-ApCpnB (6.9 kb) was transformed into E. coli BL21 Codonplus (DE3). The transformant cell successfully expressed ApCpnB, and the expression of ApCpnB (61.2 kDa) was identified through analysis of the fractions by SDS-PAGE (14% gel). The recombinant ApCpnB was purified to higher than 94% by using heat-shock treatment at $90^{\circ}C$ for 20 min and fast protein liquid chromatography on a HiTrap Q column step. The purified ApCpnB showed ATPase activity and its activity was dependent on temperature. In the presence of ATP, ApCpnB effectively protected citrate synthase (CS) and alcohol dehydrogenase (ADH) from thermal aggregation and inactivation at $43^{\circ}$ and $50^{\circ}$, respectively. Specifically, the activity of malate dehydrogenase (MDH) at $85^{\circ}$ was greatly stabilized by the addition of ApCpnB and ATP. Coexpression of pro-carboxypeptidase B (pro-CPB) and ApCpnB in E. coli BL21 Codonplus (DE3) had a marked effect on the yield of pro-CPB as a soluble and active form, speculating that ApCpnB facilitates the correct folding of pro-CPB. These results suggest that ApCpnB has both foldase and holdase activities and can be used as a powerful molecular machinery for the production of recombinant proteins as soluble and active forms in E. coli.

• 대한생식의학회:학술대회논문집
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• 2004.11a
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• pp.64-64
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• 2004

• Proceedings of the Korean Society of Plant Biotechnology Conference
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• 2006.06a
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• pp.39.1-39.1
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• 2006

• Applied Biological Chemistry
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• v.32 no.1
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• pp.23-29
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• 1989

Biochemical consequence of the accumulation in cells of superoxide $(O^{-}_{2})$ which was proposed to be probably a common chemical factor in the secondary process of the mechanism of chilling injury as well as in the visible light photodamage in cells of higher plants, has been investigated in the present work. Especially focused was the destructive effect of $O^{-}_{2}$ on the biochemical activity of mitochondria, as informations which support the suggestion that mitochondrial inner membrane is the major site of $O^{-}_{2}$ production have been collected. Mitochondria and submitochondrial particles (SMP) were prepared from soybean hypocotyls for this case study. When SMP were treated with the electrolytically produced $O^{-}_{2}$ they suffered not only inhibition of the membrane-bound enzymes as demonstrated by cytochrome c oxidase, but also lipid peroxidation of membrane as proved by malondialdehyde production. Malate dehydrogenase present in the protein extract from mitochondrial matrix was also inhibited by the $O^{-}_{2}$ treatment. These results exhibited the chaotic effect of the overproduction and accumulation of $O^{-}_{2}$ in cells under a certain abnormal circumstance such as environmental stress on the physiological function of mitochondrial; disruption of the cellular metabolic pathways and the structural integrity of membrane.

• BMB Reports
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• v.32 no.2
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• pp.203-209
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• 1999

Three-week grown Arabidopsis thaliana leaves were wounded by cutting whole leaves with a razor blade into pieces (about$3\;mm\;{\times}\;3\;mm$) submerged in various solutions, and incubated in a growth chamber for 24 h. We measured and compared activities of several enzymes such as phenylalanine ammonia-lyase (PAL), tyrosine ammonia-lyase (TAL), thioredoxin, thioredoxin reductase, thioltransferase, glutathione reductase, and $NADP^+$ -malate dehydrogenase. PAL activity was decreased in $HgCl_2$-, $CdCl_2$-, and glyphosate-treated leaf slices, and could not be detected after treatment with $CdCl_2$. TAL activity was found to be maximal in the $CdCl_2$-treated leaf slices. Activity of thioredoxin, a small protein known as a cofactor of ribonucleotide reductase and a regulator of photosynthesis, was significantly increased in the $CdCl_2$-treated leaf slices, while thioredoxin reductase activity was maximal in the $HgCl_2$-treated leaf slices. Thioltransferase and glutathione reductase activities were significantly decreased in the $HgCl_2$-treated leaf slices. $NADP^+$ -malate dehydrogenase activity remained relatively constant after the chemical treatments. Our results strongly indicate that sulfhydryl-related and phenylpropanoid-synthesizing enzyme activities are affected by chemical treatments such as hydrogen peroxide, heavy metals, and glyphosate.

• The Korean Journal of Mycology
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• v.16 no.2
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• pp.87-94
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• 1988

Electrophoretic isozyme patterns from mycelia, primordia, cap and stem of Pleurotus spp. collected in Korea were compared. Primordia, cap and stem of fruitbody showed very similar isozyme patterns but mycelial isozyme patterns were different from those of fruitbody. Isozyme patterns of malate dehydrogenase, acid phosphatase in Pleurotus ostreatus collected from different regions in Korea were similar but those of esterase, peroxidase, leucine amino peptidase and superoxide dismutase were different. Interspecific comparison of esterase isozyme patterns among Pleurotus ostreatus P. cornucopiae and, P. florida was very different and may be valuable subsidiary tool to conventional taxonomic techniques for identifying species of Pleurotus. A dendrogram by similarities of isozyme band pattern was presented.

• The Korean Journal of Zoology
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• v.15 no.3
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• pp.105-110
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• 1972

A cellulosse acetate electrophoretic survey of Korean Anura has revealed the presence of diverse lactate and malate dehydrogenase (LDH and MDH) isozymes. The pattern of LDH and MDH isozymes in the tissues of the central nervous system of the six species of Anura examined are species specific and differ from those of mammals and birds. Both Rana nigromaculata nigromaculata and Rana nigromaculata coreana have two molecular forms of LDH and MDH, respectively, with almost the same pattern. Whole brain homogenate of Rana temporaria shows also a maximum of only two LDH isozymes. Both Bufo bufo asiaticus and Bombina orientalis have five molecular forms of LDH with an entirely different spacing on the zymograms, whereas Rana rugosa has three. Two molecular forms of MDH are present in all animals examined and one band is shown in olfactory lobe and mixture of cerebellum and medulla oblongata of Rana nigromaculata nigromaculata.

• The Korean Journal of Zoology
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• v.16 no.3
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• pp.193-201
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• 1973

A cellulose acetate electrophoretic survey of Korean Anura has revealed the presence of diverse lactate and malate dehydrogenase isozymes. The LDH and MDH isozymes in the tissues of the brain, heart, stomach, skeletal muscle and liver of the six species of Anura examined show the species specific patterns which differ from those of mammals and birds. Two isozymic forms of LDH and MDH exist in both Rana nigromaculata and Rana nigromaculata coreana, respectively, with almost the same pattern. LDH of Bombina orientalis has five isozymic forms, and that of Rana temporaria ornativentris contains four isozymes. Bufo sp. has 3 to 5, and Rana rugosa has 3 to 4 isozymic bands according to the tissues. MDH's of all animals have two isozymic forms with different spacing on the zymograms.