• Journal of Preventive Medicine and Public Health
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• v.16 no.1
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• pp.79-88
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• 1983

There has been some evidence concerning the fact that trihalomethanes(THMs), toxic chlorinated compounds, may be present in drinking water. One of the important methodologies to evaluate the toxicity of THMs is to determine enzyme alteration in experimental animal tissues after treatment. This study was intended to investigate how lactic dehydrogenase(LDH) of rat tissues is affected by administration of chloroform($CHCl_3$) and dichloromonobromomethane($CHCl_2\;Br$). THMs, high dose(1/10 LD50) or low dose(1/50 LD50) of $CHCl_3$ or $CHCl_{2}Br$ were administered orally to experimental rats for 4 or 8 weeks. The treated groups of rats were sacrificed to determine LDH specific activity and isozyme pattern in various organs which were liver, thigh muscle, kidney and brain. The conclusions were obtained as follows: 1. Alteration of LDH activities and isozyme patterns were revealed before morphologic changes in tissues. 2. The LDH specific activities were increased significantly in liver and brain after administration of high concentrations of $CHCl_3$ and $CHCl_{2}Br$ for 4 weeks respectively. Otherwise, they were decreased significantly in liver, muscle and kidney after administration for 8 weeks. 3. The isozyme activities of LDH-4 and LDH-5 were increased in muscle, brain, and especially the liver. 4. It was more distinct for the decrement of LDH H-type isozyme than the increment of M-type isozyme in muscle.

• Bulletin of the Korean Chemical Society
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• v.25 no.7
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• pp.997-1002
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• 2004

A hydrogenperoxide sensor containing peroxidase extracted from horseradish was constructed and pH effect on its sensing ability was investigated. Current profiles of the biosensor with pH and the electrophoretic analysis showed that horseradish peroxidase consists of two isozymes. Assuming that it is a hypothetical twoisozyme mixture, the current profiles were deconvoluted into two Gaussians. Application of the new Michaelis-Menten equation connoting pH concept to this system enabled to find all the related dissociation constants of the isozyme-substrates and the isozyme-proton complexes and to determine pHs for the maximal isozyme activities.

• Journal of Life Science
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• v.14 no.4
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• pp.708-715
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• 2004

The lactate dehydrogenase (EC 1.1.1.27, LDH) in liver of Lempetra japonica was purified in buffer of affinity chromatography. The liver-specific $C_4$ isozyme of Gadus macrocephalus was purified by heat treatment, affinity chromatography, and DEAE-Sephacel chromatography. The liver-specific $C_4$ isozyme was eluted in a buffer containing NAD+ and was coeluted with $B_4$isozyme in plain buffer of affinity chromagraphy. Liver-specific $C_4$ isozyme in G. macrocephalus was the most thermostable, and$B_4$isozyme was more stable than $A_4$. The LDH in the fraction of pH 7.45 purified from the liver of L. iaponica by chromatofocusing was more inhibited by pyruvate than purified LDH. The optimum pH of the LDH isozyme in the liver of L. japonica was 7.5 and that of liver-specific$C_4$ isozyme was 8.5. The LDH in liver of L. japonica made complexes more with antibody against Coreoperca herzi$A_4$ and liver-specific $C_4$ than with that against eye-specific $C_4$. Therefore, the structure of the LDH in liver of L. japonica might be similarly evolved to that of subunit A and liver-specific $C_4$ isozyme in liver tissue of G. macrocephalus. The evolution rate of subunit C is faster than that of subunit A. LDH in liver of L. japonica has not one isozyme but isozymes and it was also found out to have not only subunit A and B but also subunit C.

• The Korean Journal of Zoology
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• v.31 no.3
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• pp.225-235
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• 1988

This study was carried out to compare distribution and isozyme pattern of nonspecific esterase, acid phosphatase and alkaline phosphatase on developing sparganum and adult of Spinometra erinacei by using enzyme-histochemical method and electrophoresis The sparganum and adult were recovered from rats and cat that were infected by sparganum. The results obtained were as follows: Nonspecific esterase had a strong activity in the parenchymal musculature of sparganum and adult, but no detectable level in ihe tegument. A total of 7 and 8 nonspecific esterase bands were detectable in sparganum and adult, respectively. Of these bands, band 3 and 4 were major bands in sparganum and adult. Acid phosphatase had a strong activity in the tegument and the epidermal musculature of sparganum, but no detectable level in the parenchymal musculature. A total of 3 bands were detectable in sparganum and adult. Of these bands, band 3 was major band in sparganum and adult. Alkaline phosphatase had a strong activity in the tegument and the epidennal musculature of sparganum and of adult, but no detectable level in the parenchymal musculature. A total of 2 and 4 bands were detectable in sparganum and adult. Of these bands, band 2 was major band in sparganum and adult. Based on the present results isozyme band patterns showed qualitative and quantitative changes in each tissues of sparganum and of adult during the development.

• Journal of The Korean Society of Grassland and Forage Science
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• v.12 no.1
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• pp.71-76
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• 1992

Starch gel electrophoresis was used to examine the banding pattern of Esterase isozyme in the leaf, root-nodule and seedling of four wild legume species, Trifolim repense, Glycine soja, Phaseolus nipponensis and Vigna uexillata. The number of band, enzyme activity and migrating rate of esterase isozyme varies depending on the species and tissues of legume plants. The isozyme banding pattern in the cotyledon and radicle of T. repense showed same pattern, however, the number of band were varible among the cotyledon of G. soja, P. nipponensis and V. vexzllata, respectively. Est-1 in the leaf of G. soja, V, vexillata. root-nodule of G. soja and seedling of V. vexillata expreesed the highest enzyme activity. The Est-1 showed the rapidest migrating rate among the isozymes.

• Journal of The Korean Society of Grassland and Forage Science
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• v.11 no.3
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• pp.158-161
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• 1991

Horizontal starch gel electrophoresis, follow by enzyrne-specific staining, separate and visualize several legume esterase isozyme. Using extracts prepared from cotyledon, radicle and plumule of legume seedlings germinated 5 days. The results were as follows. 1. The number and staining intensity of esterase isozyme bands varies depending on the plant species. tissues and developmental stage. 2. Bands in the cotyledon of field bean seedling expressed 4 and 1 in radicle. 3. In soybean cultivars, cotyledon of IIwangkum-kong had 3 bands and 1 band in the examined tissues of Paldal-kong and Jangkyung-kong seedling. 4. The cotyledon and radicle of french bean seedling had 3 bands, respectively. 5. The highest esterase isozyme activity appears to be expressed in the cotyledon and radicle of french bean, as indicated by intensity of stain, with the Paldal-kong particulary active.

• Journal of Microbiology and Biotechnology
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• v.20 no.9
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• pp.1266-1275
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• 2010

Isozyme and protein electrophoresis data from mycelial extracts of 27 isolates of Trichoderma harzianum, 10 isolates of T. aureoviride, and 10 isolates of T. longibrachiatum from Southern Peninsular Malaysia were investigated. The eight enzyme and a single protein pattern systems were analyzed. Three isozyme and total protein patterns were shown to be useful for the detection of three Trichoderma species. The isozyme and protein data were analyzed using the Nei and Li Dice similarity coefficient for pairwise comparison between individual isolates, species isolate group, and for generating a distance matrix. The UPGMA cluster analysis showed a higher degree of relationship between T. harzianum and T. aureoviride than to T. longibrachiatum. These results suggested that the T. harzianum isolates had high levels of genetic variation compared with the other isolates of Trichoderma species.

• Journal of Embryo Transfer
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• v.7 no.1
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• pp.31-39
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• 1992

연어류의 종간교배 실험과 LDH, MDH, IDH, $\alpha$GODH, ME 등 다섯가지 isozyme에 대한 genetic marker로서의 활용 가능성을 알아보고자 1차적으로 연어, 산천어 및 무지개송어를 이용하여 종간교배를 실시하였고 이들 세종의 isozyme pattern을 비교하였다. 교배실험은 종간교배, 및 allotriploid 구간 등 12구간으로 나누어 실시하였으며 연어 암컷과 산천어 수컷의 교배결과가 초기성장 단계적에서 가장 우수하게 나타났고이들의 allotriploid도 부활율이 28.1%로 가장 우수하였다. Genetic identification을 위한 isozyme loci 분석결과 연어와 산천어는 대부분의 loci에서 거의 찾아볼 수 없었고 무지개송어는 MDH-B와 IDH에서 다형현상을 확인할 수 있었다. 특히 MDH-B loci는 b 유전자의 출현 빈도에서 세 종간의 식별이 가능하였으며, IDH pattern을 산천어와 무지개송어의 비교에 유효한 것으로 나타났다. 이들 두 loci는 hybrid의 genotype 분석시 유용한 marker로 활용할 수 있는 가능성을 보였고, 앞으로의 어류 육종에 좋은 기초 자료로 이용될 것으로 사료된다.

• Journal of Plant Biology
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• v.18 no.4
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• pp.150-154
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• 1975

Four kinds of Nicotiana species and five varieties belonging to N. tabacum were used as materials for electrophoretic analysis of the tetrazolium oxidase isozyme to examine the taxonomic affinity among them based on the biochemical property. All the five verieties of N. tabacum showed same isozyme bands despite the fact that these varieties had notably varied characteristics including morphological traits. The band patterns were more or less different among the four species. Although N. rustica and N. tabacum were of the same genome group of AABB, their isozyme bands showed considerable difference. N. sylvestris, genome A donor of Nicotiana species, was found to be markedly different from N. tatacum in band pattern, including the absence of system 2 in N. sylvestris.

• Microbiology and Biotechnology Letters
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• v.20 no.1
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• pp.25-33
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• 1992

One acetolactate synthase isozyme which has Rf value of 0.83 on polyacrylamide gel electrophoresis was purified from Sewatia marcescens ATCC 25419 by ammonium sulfate fractionation, DEAE-Sephacel chromatography, Phenyl-Sepharose chromatography, Sephacryt S-400 gel filtration followed by native gel elution. The native molecular weight of the enzyme was determined to be 531,400 by gel filtration method, and SDS-polyacrylamide gel electrophoresis separated the native enzyme into two polypeptides having molecular sizes of 55,000 and 38,900 respectively. In kinetic parameters, $K_m$ value for pyruvate was 2.54 mM, and $V_{max}$ was 21.75 nmoie/min/mg. The enzyme showed maximal activity around pH 8.0 and optimal temperature of the acetolactate formation was $37^{\circ}C$. Feedback inhibition studies indicate that the purified enzyme is rather resistant to branched chain amino acids when compared with acetolactate synthase isozymes of plants or other enterobacteria.