• Korean Journal of Microbiology
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• v.23 no.3
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• pp.172-176
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• 1985

The present study was designed to investigate isoenzyme (ACPase, ALPase) pattern and its refulatory function between catabolically repressed and derepressed states in yeast, Saccharomyces uvarum. As the results, no other isoenzyme was detectable in acid phosphatase, but there were three isoenzyme types in aldaline phosphatase. Type "B" isoenzyme among alkaline phosphatases in catabolically repressed cell was derepressed, but in normally cultivated cell, type "C" isoenzyme was derepressed while type "B" activity was lowered. Type "B" isoenzyme could be postulated as repressible enzyme, type "A" as constityityve enzyme and type "C" as L-histidinol phosphatase, respectively, Also, it could be shown that type "B" ALPase, repressible enzyme, compensated for phosphate group supplier under catabolically repressed states. Protein profile in cytoplasmic soluble fraction of exponential phase cell was characterized by negative charged protein.

• 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.

• The Korean Journal of Pharmacology
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• v.16 no.2 s.27
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• pp.15-24
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• 1980

[${\alpha}$]-Amylase catalyses the hydrolysis of starch, glycogen, and related poly- and oligosac-charide by random cleavage of ${\alpha}$-D-(l-4) glucan linkage. In man large amounts of amylase are secreted into the digestive tract by the salivary and exocrine pancreatic gland, minimal amount being produced also in other tissues. It has been known that ${\alpha}$-amylase exists in multiple molecular forms, isoenzyme which can be separated from each other because of difference in their physicochemical properties. By using various methods, several groups of investigator have separated the many isoenzyme in serum, saliva and pancreatic juice. Furthermore, changes of the normal serum isoenzyme pattern is diagnostically useful even when the total serum enzyme activity is noninformative, such as the clinical use of isoenzyme of serum lactate dehydrogenase. Procarboxypeptidase-A which is one of the pancreatic enzymes is also present as isoenzymes. Four forms of procarboxypeptidase-A haye been found in the bovine enzyme and three forms of the porcine enzyme. In human pancreatic juice four forms of procarboxypeptidase-A isoenzyme were found by isoelectric focusing method. Recently, the so-called isoamylase analysis was developed for the diagnostic use of amylase in pancreatic diseases. In alcohotic patients, the serum concentration of pancreatic isoamylase is subnormal and this lowered activity provides strong evidence for pancreatic exocrine insufficiency. The purpose of this study was to elucidate the variations of the isoenzyme of amylase and procarboxypeptidase-A in serum, saliva and pancreatic juice of the experimental animals. The results are as follow. 1) Three main forms of isoenzyme of amylase by isoelectric focusing were found in pancreatic juice of normal rabbit. However, many new bands were appeared in the pancreatic juice of cholic acid administered animal intravenously while the infusion of cholic acid or elastase into pancreatic duct produced the decrease of number of the fractions on the isoelectric focusing. In the case of serum isoenzyme from normal animal, two major and a few minor isoamylases were observed. By injecting alcohol intravenousely the fractions of serum isoamylase were significantly decreased and in contrary to the pattern in the pancreatic juice the infusion of cholic acid or elastase into pancreatic duct exhitited a significant decrease of the isoenzyme of amylase fractions. In saliva from normal animal three main isoamylase were produced of the administration of alcohol. 2) In the case of procarboxypeptidase-A isoenzyme, two major fractions which have isoelectric point at 6.2 and 6.4 and other two minor bands were observed in the pancreatic juice of normal rabbit. By the treatment of the juice with trypsin, only one band was produced on the isoelectric focusing. No procarboxypeptidase was appeared on the electrofocusing by the infusion of cholic acid or phospholipase A into the pancreatic duct of rabbit. However, a single major fraction of procarboxypeptidase-A was appeared at 3 hr after simple ligation of the pancreatic duct. No significant changes were observed in the juice of the alcohol or cholic acid administered group.

• Journal of Veterinary Clinics
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• v.18 no.4
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• pp.390-396
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• 2001

CKP isoenzymes have a high level of efficaciousness as diagnostic and prognostic aids in various diseases. There is not any report on the total activity of CPK of non-human primates, let alone CPK isoenzyme patterns, in Korea. In this study, total activities and isoenzyme patterns of CPK were measured to obtain their reference values in domestically reared common marmosets, crab-eating macaques and Japanese macaques. We observed remarkable different values of serum total CPK from the primates used in this experiment. Serum CPK activities of Japanese macaques and crab-eating macaques were 275.8$\pm$158.1 IU/l and 396.7$\pm$697.4 IU/l, respectively, whereas those of common marmosets showed much higher value of 618.8$\pm$1,117.6 IU/l. In all common marmosets and crab-eating macaques, only CPK$_3$ ws observed. In five out of eight Japanese macaques, CPK$_3$ was the sole fraction but two animals showed CPK$_1$ and CPK$_3$ isoenzymes, and the remaining one had CPK$_2$ and CPK$_3$ fractions. There were some discrepancies in the pattern and ratio of isoenzyme fractions in Japanese macaques. In conclusion, values such as CPK and CPK isoenzyme patterns of investigated for the first time form non-human primates reared in Korea, could be reference values for the optimal diagnosis and therapy diseases of the corresponding animal species.

• Proceedings of the Zoological Society Korea Conference
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• 1994.10a
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• pp.194.1-194
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• 1994

• Korean Journal of Plant Tissue Culture
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• v.22 no.2
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• pp.105-110
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• 1995

The experiment were carried out to obtain a somatic hybrid through protoplast fusion between P.hybrid and N. sanderae. The isoenzyme pattern he chromosome number and the phonotype were observed for genetic study on the regenerants obtained from the fusion product cultures. Putative somatic hybrids possessed all the bands that appeared in both mother plane. A specific band was found on the top of the banding pattern which was assumed to be a marker band of somatic hybrid between two genera. Aspartate amninotransferase isoenzyme bands which were found in both mother plane were also revealed in the putative somatic hybrids or deleted in the upper part of H. sanderae band pattern. The chromosome number of P.hybrida was 2n=14, while N, sanderae was 2n=18,but the number of the putative somatic hybrids ranged from n=32 to 36. The phonotype of putative somatic hybrids was intermediate of the mother plants.

• Korean Journal of Microbiology
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• v.14 no.1
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• pp.39-47
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• 1976

This experiment was designed to study the effects of temperature on the peroxidase isoenzymes of a mesophilic microorganism, Escherichia coli (grown within biokinetic zone). Optimum temperature for the growth of E. coli was $37{\circ}C.$ Three different temperatures, 20, 30 and $40{\circ}C,$ were selected. And the isoenzyme patterns of peroxidase of E. coli, growth respectively at each temperature, were analysed by disc electrophoresis. The sample of 20.deg.C showed 4 bands, that of 30.deg.C, 5 bands and that of 40.deg.C, 6 bands. Two dark bands (higher molecular weight, 56,000 and 54,000) and two light bands (lower molecular weight, 11,500 and 10,000) were constant at all samples. But two intermediate bands (M.W.44,000 and 34,000) were variable ; at $20{\circ}C,$ no banding pattern, one band 9M.W. 34,000) only at $30{\circ}C,$ and at $40{\circ}C$ two bands were appeared. And the shifts of growth temperatures between 30.deg.C and 40.deg.C showed the alteration of the isoenzyme patterns ; the isoenzyme patterns of the smaple of tmeperature shift from $30{\circ}C$ to $40{\circ}C$ were same as that of 40.deg.C and vice versa.

• The Journal of the Korean dental association
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• v.10 no.2
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• pp.97-107
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• 1972

백서에 1000R의 $Co^{60}$-gamma선을 전신 조사 후 시간에 따른 LDH isoenzyme의 Pattern과 그의 활성도의 변화를 관찰한 바 다음과 같은 결론을 얻었다. 1. 조사후 72시간에 LDH-1와 LDH-4의 뚜렷한 Pattern을 나타내어, 이는 치수의 energy 대사가 염기성과 호기성 대사과정을 동시에 행함을 의미한다. 2. LDH의 총활성도는 조사후 24시간에 현저히 감소하였으나 72시간 후에는 거의 비조사군에 가까워졌다.

• Korean Journal of Plant Tissue Culture
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• v.24 no.1
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• pp.57-61
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• 1997

We investigated changes in the superoxide dismutase (SOD) activity and SOD isoenzyme pattern in suspension cultures of tomato (Lycopersicon esculentum), which were compared with those of intact tomato plants. two grams (fr wt) of cells subcultured at 15-day intervals were inoculated into 50 mL MS medium containing l mg/L 2,4-D and 30 g/L sucrose in a 300 mL flask and maintained at $25^{\circ}C$ in the dark (100 rpm). The cell growth reached a maximum at 20 days after subculture (DAS), followed by a rapid decrease with further cultures. The cell colour changed from white to black from 23 DAS. The intracellular SOD activity (units/g cell dry wt) was significantly increased from 23 DAS and reached a maximum at 28 DAS (52,400 units), followed by a decrease with further cultures, whereas the extracellular SOD activity showed a maximum at 25 DAS (27,800 units/50 mL medium). The total SOD activity per flask showed a maximum at 25 DAS (35,700 units), in which the extracellular SOD activity occupied about 75%. The tomato cultured cells had four SOD isoenzymes and their patterns were well correlated with SOD activity without a qualitative change during the cell cultures. The intact tomato plants had an additional CuZnSOD isoenzyme, showing the different isoenzyme patterns from cultured cells.

• 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.