• BMB Reports
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• v.35 no.2
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• pp.220-227
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• 2002

Two aspartate aminoransferase (EC 2.6.1.1) isoenzymes (AAT-1 and AAT-2) from Lupinus albus L. cv Estoril were separated, purified, and characterized. The molecular weight, pI value, optimum pH, optimum temperature, and thermodynamic parameters for thermal inactivation of both isoenzymes were obtained. Studies of the kinetic mechanism, and the kinetics of product inhibition and high substrate concentration inhibition, were performed. The effect of some divalent ions and irreversible inhibitors on both AAT isoenzymes was also studied. Native PAGE showed a higher molecular weight for AAT-2 compared with AAT-1. AAT-1 appears to be more anionic than AAT-2, which was suggested by the anion exchange chromatography. SDS-PAGE showed a similar sub-unit molecular weight for both isoenzymes. The optimum pH (between 8,0 and 9.0) and temperature ($60-65^{\circ}C$) were similar for both isoenzymes. In the temperature range of $45-65^{\circ}C$, AAT-2 has higher thermostability than AAT-1. Both isoenzymes showed a high affinity for keto-acid substrates, as well as a higher affinity to aspartate than glutamate. Manganese ions induced an increase in both AAT isoenzymes activities, but no cooperative effect was detected. Among the inhibitors tested, hydroxylamine affected both isoenzymes activity by an irreversible inhibition mechanism.

• BMB Reports
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• v.32 no.5
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• pp.506-510
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• 1999

The newly-found thiol peroxidases (TPx) with a conserved cysteine as the primary site of catalysis are capable of catalyzing the thiol-dependent reduction of peroxides. However, the cellular distributions of the isoforms remain poorly understood. As a first step in understanding the physiological functions of the TPx isoforms, we examined the cellular and tissue distribution of the isoenzymes in various bovine tissues. The tissue distributions of TPx isoenzymes indicate that two types of TPx are widely distributed throughout all of the tested tissues. These two forms are the predominant proteins, with levels of the proteins being quite different from each other. The level of predominant TPx proteins, named type II (TPx II) and type V (TPx V), appeared to be very different with respect to tissue type. The cellular distribution and level of TPx isoenzymes also varied with the types of cells. Immunoblot analysis of the mitochondrial and cytosol fractions from various tissues indicates that TPx III is a unique mitochondrial form. Based on the different tissue and cellular distribution of TPx isoenzymes, we discuss the physiological function of TPx isoenzymes, especially the ubiquitous TPx II.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.6
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• pp.954-958
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• 1994

The bleaching effect of chlorophyll a by two lipoxygenase isoenzymes (LOX-1, LOX-2) isolated from potato tuber(variety DEinma ) was studied. In the presence of LOX-1 or LOX0-2 with linoleic acid chlorophyll a bleaching occurred during two isoenzymes-mediated oxidation of linoleic acid. Chlorophyll a bleaching porceeded with decreasing in the formation of conjugated dienes form linoleic acidyb LOX-1 and LOX-2 . In the presence of chlorophyll a, LOX-2 showed a markable decrease inproduction of conjugated dienes from linoleic acid and a higher chlorophyll a bleaching activity. compared with LOX-1. These results suggest chlorophyll-bleaching reaction required intermediates formed during the peroxidation of linoleic acid by lipoxygenase isoenzymes, thus preventing formation of conjugated dienes.

• Journal of Veterinary Clinics
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• v.9 no.2
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• pp.417-426
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• 1992

Total CPK activities and CPK isoenzymes fractions of the sera and some organ tissues of dogs were examined to acquire the basic data of canine CPK available in clinical practice. In addition fluctuation of serum total CPK activities and CPK isoenzymes fractions is artificially induced canine myocardial infarctino were investigated to know the availabity of them as indicators for the diagnosis of myocardial infarction. For the determination of serum total CPK activities, total 22 clinically healthy dogs(7 to 30 months old, 15 of female and 7 of male) were used and 15 out of 22 dogs were used for the determination of serum CPK isoenzymes fractions. For the determination of total CPK activities and CPK isoenzymes fractions. some organ tissues (the hearts, skeletal muscles and brains )from 3 dogs were examined. For the fluctuation of total CPK activities and CPK isoenzymes fractions in the sera from artificially induced canine acute myocardial infarction, 3 dogs of coronary artery ligated experimental group and 3 of control group were used. The results obtained were as follows ; 1. Serum total CPK activities of normal dogs were 106.2${\pm}$29.9(31.3∼148.1)IU/$\ell$. 2. The pattern of serum CPK isoenzymes fractions in normal dogs was high with decreasing order of CK$_1$>CK$_3$>CK$_2$. 3. Total CPK activities of organ tissues were high with decreasing order of the skeletal muscles > the hearts > the brains. 4. The pattern of CPK isoenzymes fractions of the organ tissues was high with decreasing order of CK$_3$>CK$_2$ in the hearts and only CK$_3$(100%) was detected in the skeletal muscles. Further they were high with decreasing order of CK$_1$>CK$_3$>CK$_2$ in the trains. 5. Serum total CPK activities in experimental group were changed with higher values than those of control group. 6. In the fluctuation of serum CPK isoenzymes fractions the CK$_1$ CK$_2$ and CK$_3$ values were changed with higher values than those of control group. 7. It was become clear that the finding of Increase of serum total CPK activities, and CK$_2$ and CK$_3$ was important for the diagnosis of myocardial infarction.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.777-784
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• 1993

The bleaching effect of potato lipoxygenase Isoenzymes on ${\beta}-carotene$ was studied. Two lipoxygenase Isoenzymes(LOX-1, LOX-2) from potato tuber were purified by CM-cellulose, DEAE-cellulose ion exchange chromatography. LOX-1 and LOX-2 seemed to have bleaching effect on ${\beta}-carotene$ in the presence of linoleic acid, which the decrease in the formation of conjugated dienes. LOX-2 was founded to have a greater pigment bleaching activity than that of LOX-1.

• Journal of Veterinary Clinics
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• v.9 no.2
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• pp.433-449
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• 1992

Total CPK activities and CPK isoenzymes fractions of the sera and tissues were examined to obtain the physiological basic data of ruminant available in veterinary clinical practice. For the sera total CPK activities and CPK isoenzymes fractions, total 39 clinically healthy Korean native goats (3 to 10 months old, IS of female and 18 of male) and 6 of Korean native goats (1 to 2 years old, 3 of female and 3 of male) were used. Seventeen Korean native cattle (3 to 6 years old, 10 of female and 7 of male) and 27 Holstein-Friesian cattle (2 to 8 months old, 7 of female and 3 to 12 years old, 20 of female) were also examined for the sera total CPK activities and CPK isoenzymes fractions. For the total CPK activities and CPK isoenzyme fractions, 3 of female Korean native goats (7 months old), 3 of female Korean native cattle (2 years old) and 3 of dairy cattle (2 years old, 2 of female and 1 of male) were used. The tissues examined were the cerebrum (2 of Korean native cattle), spinal cord (1 of Korean native cattle), heart, lung, diaphragm, reticulum, liver, spleen, kidney, jejunum. colon and femoral muscle. The results obtained were as follows : 1. In Korean native goats less than 1-year-old. serum total CPK activities were 67.8${\pm}$17.7(39.0~96.5) IU/$\ell$ in female and 63.4${\pm}$19.0(28.7~94.4) IU/$\ell$ in male. Further they were 67.0${\pm}$5.3(59.5~70.7) IU/$\ell$ and 54.5${\pm}$11.1(39.1~69.4) IU/$\ell$ in female and male Korean native goats over 1-year-old, respectively. Serum total CPK activities of female were slightly higher than those of male. Significance between age and sex was not found. 2. Serum total CPK activities were 56.8${\pm}$19.7(27.6~90.5) IU/$\ell$ and 65.6${\pm}$10.8(52.8~78.0) IU/$\ell$ in female and male Korean native adult cattle, respectively, Serum total CPK activities of male were slightly higher than those of female, but they were not significant 3. Serum total CPK activities we,e 72.5${\pm}$8.2(57.2~83.2) IU/$\ell$ and 60.8${\pm}$12.5(42.7~80.6) IU/$\ell$ in calves and adult of dairy acttle, respectively. Serum total CPK activities of calves were significantly higher than those of adult(p<0.05). 4. In Korean native goats less than 1-year-old, serum CPK isoenzymes fractions were high with decreasing order of MM>MB>BB and MM>BB>MB in female and male, respectively. Further they were high with decreasing order of MM>MB>BB and MM>B8>MB in female and male Korean native goats over 1-year-old, respectively. The main fractions of CPK isoenzymes were MM in sera of Korean native goats. 5. Serum CPK Isoenzyme fractions were high with decreasing order of MM>MB>BB In both female and male of Korean native cattle. The main fraction among them was MM. 6. Serum CPK isoenzymes fractions were high with decreasing order of MM>BB>MB in both calves and adult of dairy cattle. The main fraction among them was MM. 7. Total CPK activities were high with decreasing order of the femoral muscle>kidney>reticulum>diaphragm>liver>spleen>heart>colon>lung>jejunum in Korean native goats. 8. Total CPK activities were high with decreasing order of the spinal cord >cerebrum>femoral muscle>reticulum>kidney>liver>spleen>diaphragm>lung>colon>heart>jejunum in Korean native cattle. 9. Total CPK activities were high with decreasing order. of the femoral muscle >liver>retoculum>kidney>heart>colon>lung>spleen>jejunum>diaphrasm in dairy cattle. 10. The pattern of the cardiac CPK isoenzymes fractions was identical in Korean native goats, Korean native cattle and dairy cattle. They were high in the order of MM>MB without BB fractions and the main fraction was MM. 11. The pattern of the pulmonary CPK isoenzymes fractions was the same Korean native goats, Korean native cattle and dairy cattle. They were high with decreasing order of MM>MB>BB and the main fraction among them was MM. 12. The pattern of CPK isoenzymes fractions of the diaphragm was Identical in Korean native goats and Korean native cattle. They were high with decreasing order of MM >BB >MB except dairy cattle (MM>MB>BB) but the main fraction among them was MM. 13. The pattern of the reticular CPK isoenzymes fractions was identical in Korean native cattle and dairy cattle. They were high with decreasing order of BB >MM >MB except Korean native goats(BB>MB>MM) but the main, fraction among them was BB 14. The pattern of the hepatic CPK isoenzymrs fractions was identical in Korean native cattle and dairy cattle. They were high with decreasing order of MB >BB >MM except Korean native goats(MB>MM>BB)but the main fraction was MB. 15. The splenic CPK isoenzymes fractions showed different pattern. They were high with decreasing order of MB>BB>MM, MM>BB>MB and BB>MB>MM in Korean native goats, Korean native cattle and dairy cattle, respectively. The main fraction among them was different from each other. 16. The pattern of the renal CPK isoenzymes fractions was identical in Korean native cattle and dairy cattle. They were high with decreasing order of MM >MB>BB except Korean native goats(BB>MB>MM). 17. The CPK isoenzymes fractions of the Jejunums showed different pattern. They were high with decreasing order MM>MB>BB, MM>BB>MB and BB>MM>MB in Korean native goats, Korean native cattle and dairy cattle, respectively. The main fractions were MM In Korean native goats and Korean native cattle, and BB in dairy cattle. 18. The colonic CPK isoenzymes fractions showed different pattern. They were high with decreasing order of MM>MB>BB, MM>BB>MB and BB>rrfB>MM in Korean native goats, Korean native cattle and dairy cattle, respectively. The main fractions were MM in Korean native goats and Korean . native cattle, and BB in dairy cattle. 19. The cerebral CPK isoenzymes fractions were high with decreasing order of BB >MM without MB detected in Korean native cattle and those of spinal cord were high with decreasing order of BB >MM >MB. The main fractions in both cerebrum and spinal cord were BB.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.6
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• pp.95-95
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• 1994

• Korean Journal of Veterinary Research
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• v.29 no.4
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• pp.461-467
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• 1989

The activity of lactate dehydrogenase in plasma and various tissues(skeletal muscle, cardiac muscle, liver, lung, kidney and spleen) of Korean native cattle in a Chonju abattoir, the Breeding Stock Farm and Animal Farm of Chonbuk University was determined by using ultra violet method. Using polyacrylamide gel electrophoresis, the lactate dehydrogenase isoenzyme distrimution of plasma and various tissues in Korean native cattle was studied. The plasma lactate dehydrogenase activity of Korean native cattle was $554.80{\pm}92.70IU/l$ and the lactate dehydrogenase activity of male plasma was $543.96{\pm}97.89IU/l$, which was lower than that of female plasma, $579.19{\pm}78.09IU/l$. The plasma lactate dehydrogenase activity of calf was $557.31{\pm}110.27IU/l$ and was no significantly different from that of adult Korean native cattle. But the range of calf lactate dehydrogenase activity was larger than that of adult Korean native cattle. In tissues, the lactate dehydrogenase activity was decreased in order of lung, kidney, spleen, liver, heart and skeletal muscle. The lung had the greatest activity and the skeletal muscle had the least. Lactate dehydrogenase isoenzymes in plasma and tissues were found to have a characteristic distribution and quantitative isoenzyme patterns. In plasma, the LDH1 usually had the greatest activity and other isoenzymes showed a decreasing tendency in order of LDH2, LDH3, LDH4 and LDH5. The distribution of lactate dehydrogenase isoenzymes had a wide variation in tissues. But the distribution of LDH isoenzymes in plasma was similar to that in kidney, and also cardiac muscle and spleen had similar pattern in LDH isoenzymes distribution.

• Korean Journal of Plant Resources
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• v.12 no.3
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• pp.234-239
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• 1999

The isoenzyme patterns and activities of superoxide dismutase(SOD) were investigated from leaves of Araliaceae plants. Of the eight isoenzymes, two isoenzymes(SOD 4 and SOD 6) were prevalent to leaves of Araliaceae plants. The patterns of these two isoenzymes were most various in the leaves of Acanthopanax senticosus for. inermis, while their activity was highest in the leaves of A. koreanum. These two isoenzymes were respectively identified as Fe-SOD and CuZn-SOD, based on selective inhibition with KCN or$H_2O_2$. The SOD isoenzyme patterns did not differed among stem barks, root barks and leaves of A. koreanum. However, the activities of Fe-SOD and CuZn-SOD were higher in the root bark and in leaves, respectively. Both of Fe-SOD and CuZn-SOD were stable for 1 hr at 30-4$0^{\circ}C$, while unstable above 5$0^{\circ}C$.

• The Journal of the Korean dental association
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• v.10 no.1
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• pp.15-21
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• 1972

In the periodic amputated rat incisor pulp, the distribution of five isoenzymes of lactic acid dehydrogenase was evaluated and the total LDH activity was assayed. This study hs established the followings; 1) It demonstrates the existence of five distinct isoenzymes of LDH, with LDH-1 and LDH-2 predominating, in the rat incisor pulp. 2) The total LDH activity in periodically amputated rat incisor pulp is markedly increased as compared to the normal rat incisor pulp. 3) It is possible that the periodic amputation of tooth effects the pattern of LDH isoenzymes in the pulp, especially LDH-1 and LDH-2 region.