• The Korean Journal of Pesticide Science
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• v.11 no.3
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• pp.179-185
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• 2007

Esterase isozymes were investigated from digestive juice of M. saltuarius adults after pesticide treatment. Twelve esterase isozymes were separated on 12% native-PAGE gel and stained with three different substrates(${\alpha}$-naphthyl acetate, ${\beta}$-naphthyl acetate, and ${\alpha}$-naphthyl butyrate). Interestingly, the isozyme of Est1(${\alpha}$-naphthyl acetate) was strongly inhibited by the carbofuran and methomyl. The Est1 activity was completely inhibited by the chlorpyrifos and partially inhibited by methidation about 70 %. In addition, eserine suppressed esterase isozyme activities of Est1 about 70% and isozyme activities of Est2, Est3, and Est4 were weakly inhibited. ${\alpha}$-pinene did not suppressed esterase isozyme activities but activities of esterases were very weakly inhibited in camphor and bornyl acetate.

• The Korean Journal of Mycology
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• v.18 no.4
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• pp.209-217
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• 1990

The influence of cellulosic and hemicellulosic substrates on the production of cellulase and xylanase complexes in Aspergillus niger was investigated. The culture conditions with different substrates exhibited profound effects on the level of endoglucanase (CMCase), ${\beta}-glucosidase$, endoxylanase and ${\beta}-xylosidase$, and on their isozyme patterns. However, intracellular and extracellular isozyme patterns of cellulase and xylanase complexes were qualitatively identical and appeared to be simultaneous in the early growth phase. Prolonged incubation led to the increase in the concentrations of isozymes with a little changes in the relative proportions of those isozymes. These results suggest that the biosynthesis of cellulase and xylanase complexes in A. niger is coordinately regulated at the level of induction. Moreover, multiple forms of extracellular cellulase and xylanase complexes seem to be the outcome of specific gene expression and should not be considered solely as the consequence of post-secretional modification of synthesized enzymes.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.39 no.3
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• pp.211-215
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• 1994

Lipoxygenase is involved in the formation of certain undesirable flavors of soybean products. Three isozymes(L-1, L-2 and L-3) of lipoxygenase have been identified in soybean seeds, and the three types of mutants lacking L-1, L-2 and L-3, respectively, were detected in the 1980's. In this paper, lipoxygenase activity was measured to investigate the response of lipoxygenase in organs and tissues during soybean development. There was no tendency according to genotypes between lipoxygenase lacking mutants and normal soybeans in lipoxygenase activity of leaf at $V_3$ and $V_5$ stage. Likewise, pod wall lipoxygenase was no difference among genotypes tested at R$_{6}$ stage. Seed coat lipoxygenase activity was similar among the lipoxygenase lacking mutants, while normal soybean was lower as compared with that of the lipoxygenase lacking mutants. Embryo and cotyledon lipoxygenase activity in the lipoxygenase lacking mutants was much lower than that of normal soybean, also there was large difference among lipoxygenase lacking mutants. Thus, the lipoxygenase null mutant showed very weak value although the lacking L-3 mutant had a large effect on developing embryo lipoxygenase activity. It was suggested that soybean lipoxygenase isozymes expressed in embryo may be different from those expressed in the pod wall and leaf tissues.

• Journal of Life Science
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• v.18 no.2
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• pp.264-272
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• 2008

The lactate dehydrogenase (EC 1.1.1.27, LDH) isozymes in tissues from Acanthogobius hasta were characterized by biochemical, immunochemical and kinetic methods. The activities of LDH in skeletal muscle and eye tissues were 65.30 and 53.25 units, but LDH activities in heart and liver tissues were very low. LDH/CS (EC 4.1.3.7, citrate synthase) in skeletal muscle was the highest as 22.29. Specific activities of LDH in brain, eye and skeletal muscle were 56.45, 38.04 and 11.0 units/mg, respectively. The LDH isozymes in tissues were separated by polyacrylamide gel electrophoresis after immunoprecipitation with antiserum against $A_4,\;B_4$ eye-specific $C_4$ and liver-specific $C_4$. LDH $AC_4$ isozymes were detected predominantly in skeletal muscle, brain and eye tissues, and $B_4$ isozyme was detected in heart. Anodal eye-specific $C_4$ and cathodal liver-specific $C_4$ were coexpressed in A. hasta. The eye-specific $C_4$ isozyme showed higher activity in eye tissue, but liver-specific $C_4$ isozyme showed lower activity in liver. As a result, one part of molecular structures in $A_4\;and\;C_4,\;A_4\;and\;B_4$, and eye-specific $C_4$ and liver-specific $C_4$ were similar, but in $B_4\;and\;C_4$ were different with each other. Therefore the subunit A may be conservative in evolution, and the evolution of subunit B seems to be faster than that of subunit A. The LDH $A_4$ isozyme of skeletal muscle was purified in the fraction from elution with NAD+ containing buffer of affinity chromatography and eye-specific $C_4$ isozyme was eluted right after $A_4$, so the structure of eye-specific $C_4$ isozyme is similar to $A_4$. And LDH activity remained 35.22-43.47% as a result of the inhibition by pyruvate, the Michaelis-Menten constant values for pyruvate was 0.080-0.098 mM, and Vmax were 153.85 units, 35.09 units in skeletal muscle and eye, respectively. Also the $B_4$ isozyme was the thermo-stablest and $C_4$ was stabler than $A_4$ isozyme. The optimum pH of LDH was 6.5. The results mentioned above indicate that isozymes in tissues showed the properties between LDH $A_4\;and\;B_4$ isozyme as A. hasta was adapted to hypoxic conditions. Also LDH seems to function more effectively under anaerobic condition because LDH in skeletal muscle and eye tissues have high affinity for pyruvate.

• Journal of the Korean Society of Food Science and Nutrition
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• v.33 no.2
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• pp.262-270
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• 2004

It is well known that long-term heavy ethanol intake causes alcoholic dementia, cerebellar degeneracy or Wernicke-Korsakoff syndrome and aggravates the conditions of many other neuro-psychotic disorders. Recently it is indicated that protein kinase C (PKC) plays an important role in the action of ethanol and in the neuro-adaptational mechanisms under chronic ethanol exposure. In order to investigate the effect of ethanol on PKC isoforms levels within the range of not showing any cytotoxicity, B103 neuroblastoma cell line trans-formed from murine central nervous system was employed and western blot analysis was carried out by using PKC isoform-specific antibodies. The changes of PKC-$\alpha$, ${\gamma}$, $\varepsilon$ and ζ level in the range of ethanol concentration 50∼200 mM were examined at the exposure time 1, 2, 8, 18 and 24 hrs in both cytosolic and membrane fraction. A typical ethanol concentration inducing the PKC isozymes was 100 mM, and the transforming time ranges of PKC isozymes could be considered as two different parts to each PKC isoform such as initial (0∼2 hrs) and prolonged (8∼24 hrs) stages. PKC-${\gamma}$ and PKC-$\varepsilon$ were clearly induced during the prolonged stages in cytosol at 18 hrs, and membrane fraction at 8 hrs and 18 hrs, respectively. On the other hand the PKC-$\alpha$ and PKC-ζ isozymes were largely induced in the prolonged stages at 18 hrs and 24 hrs, where the PKC-$\alpha$ isozyme was induced in both cytosol and membrane fractions at 200 mM ethanol concentration while the PKC-ζ isozyme was induced only in the membrane fractions at 100,200 mM. At 200 mM ethanol concentration of 24 hrs incubation in the prolonged stage, the PKC-$\alpha$ was maximally induced by 150% of the control values whereas the PKC-${\gamma}$ was significantly decreased to 47% of the control values. These results suggest that 100∼200 mM ethanol may modulate the signal transduction and neurotransmitter release in the central nervous system through the regulation of PKC isozymes, and the action of these isoforms may act differently each other in the cell.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.31 no.3
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• pp.375-382
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• 1986

This study was carried out to obtain the basic information for the clarification of spring growth habits mechanism of naked barleys. The isozyme patterns and activities of peroxidase in the young spike and leaf blade were analyzed during the differentiation and development of young spike. The characteristic differences between the normal and rosetted type were in c and g isozymes in young spike, and in i isozyme in the leaf blade. In the normal type, c and i isozymes disappeared at the stage of spi-kelet differentiation, g isozyme at the stage of flolet differentiation. But, in the rosetted type, those three isozymes remained in dark stained condition until the time of final sampling. Especially, those three isozymes were higher in the rosetted type than those in the normal type even at the stage of bract differentiation(BDS), just prior to the reproductive stage. The activities of peroxidase decreased slowly after BDS in the young spike and leaf blade in the normal type, While, in the rosetted type, increased linearly, and the degree of increasing was remarkable in the young spike. It was interesting that the degree of activities in young spike was higher in the rosetted type than that in the normal type even at BDS. From the above results, the remarkable differences of the isozyme patterns and activities at BDS between the normal and rosetted type were considered to be the physiological expression of the varieties concerned with the degree of spring growth habits.

• Parasites, Hosts and Diseases
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• v.34 no.1
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• pp.69-78
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• 1996

This study was done to investigate the enzyme-histochemical localization and characteristics of alkaline and acid phosphatase related with metabolism in sparganum and adult of Spirometrn erinacei. By the enzyme-histochemical assay, the alkaline and acid phosphatases were localized in the tegument and subtegumental musculature of sparganum and adult, but not in the parenchyma. The activities of alkaline phosphatase were stronger in the tegument than in the subtegumental musculature, and activities of acid phosphatase were stronger in the tegument of adults than those of sparganum. The 2 isozymes of alkaline and acid phosphatases were separated from s-sparganum (from snake) and r-sparganum (from experimentaly infected rats) respectively but 4 isozymes of Alp and 3 isoxymes of Acp were separated from adult worms by electrophoresis. In isogyme Alp, the 661)a was the common isozyme, but 130 kDa isozyme of Acp was the common isozyme in spargana and adult worms. By isoelectrofocusing, 4 isozymes (PI 7.9, 7.7, 6.5 and 6.3) and 2 isozymes (PI 7.9 and 7.7) of alkaline phosphatase were separated from adults and spargana respectively. In the stability against heat, activity of alkaline phosphatase was denatured perfectly after heating at 90℃ for 40 seconds. The optimum pH and temperature for activity of alkaline phosphatase were about pH 10 and 50℃, respectively. The maximum activity (unit) of alkaline phosphatase was 22.0 in s- sparganum,25.0 in r-sparganum and 215.0 in adult worms, so that the maximum activity was revealed higher in adults than spargana. As the result from above, we observed that alkaline and acid phosphatases were functioned mainly in the tegument and subtegumental musculature , and the isoxymes of phosphatase were activated differently according to habitat of the parasites. The spargana and adult worms carry out the pafasitism by adapting thenlselves to parasitic circumstance loth these emxymes.

• Parasites, Hosts and Diseases
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• v.21 no.1
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• pp.41-48
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• 1983

The activity and distribution of aspartate aminotransferase (EC 2.6. 1. 1) and alanine aminotransferase (EC 2.6.1.2) in adult Fascicle hepatica have been studied. Fasciola hepatica was fractionated by differential centrifugation into nuclear, mitochondrial and cytosolic fractions. The activity of GOT and GPT was measured by the method of Reitman and Frankel. Isozyme patterns of those enzyme were also examined by DEAE-cellulose column chromatography. The results obtained were as follows; 1. The activity of aspartate and alanine aminotransferase was about 0.55 unit and 0.92 unit per 1g of Fascicle hepatica, respectively. 2. The activity of those enzymes was relatively low compared with those in mammalian tissues. 3. The distribution of aspartate aminotransferase in the subcellular organelles showed that 71% of the activity was in cytosolic, 24% in mitochondrial and 5% was in nuclear fraction. 4. About 22% of the total alanine aminotransferase activity was found in the mitochondrial fratstion, about 66% in the cytosolic fraction. 5. Aspartate aminotransferase from cytosolic fraction was separated into two types of isozymes, whereas alanine aminotransferase from cytosolic fraction gave only one active peak on DEAE-cellulose column chromatography.

• Journal of the Korean Society of Tobacco Science
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• v.4 no.2
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• pp.3-10
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• 1982

This experiment was conducted to study the effect of soil water potenial on the growth and internal changes of stressed plants. The experimental imposition of soil water potential ( $\Psi$soil) were -0.1 to -0.2, -0.2 to -0.5, -0.5 to -3.0, -3.0 to -10.0 bar respectively. During water stress all growth rates were depressed, and the most sensitive period to water stress was found to be 10 to 25 days after transplanting. The water potential of leaf was declined rapidly within 12 hours after with holding of water. Nitrate reductase activity was decreased progressively as water deficit was built up in tobacco leaves, but the activity of alpha- amylase and super contents were increased. There were differences in peroxidase isozyme patterns between tile control and water stressed plant. New isozymes started to appear as tobacco leaf water potential decreased.

• Journal of Plant Biology
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• v.36 no.4
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• pp.307-312
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• 1993

In germinating pea, contents of enodgenous polyamine in the leaf and stem were determined, and protein content, peroxidase activity and pattern of isozymes were examined in the leaf treated with polyamines. During growth of the pea for 14 days in light condition, the polyamines in leaf and stem showed the highest level at the 5th day, and were decreased rapidly at the 7th day, kept almost constant level since then. The putrescine level was relatively higher than those of spermidine and spermine, and cadaverine was also detected. On the other hand, in the leaf treated with spermine (0.01 mM) protein content increased about 250% than that of the control, the peroxidase activity increased ore than 100% in spermine of 0.01 mM and 0.1 mM. In treating with putrescine of 0.1 mM the pattern of peroxidase isozyme appeared 4 new cathodic bands (pI 4.8, 5.6, 5.9 and 6.8) compared with the control, the clear cathodic bands (pI 5.6, 5.9, 6.4 and 6.6) were also observed in spermine of 0.1 mM. These results suggest that polyamines were important factor in the differentiation of pea at the early stage of germination.