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지은정,Jhee, Eun-Chung 생화학분자생물학회 1974 한국생화학회지 Vol.7 No.2
가토 적혈구로부터 막 분획을 분리하여 막 결합 효소인 acid phosphatase의 성상을 구명하였다. 이 효소는 적혈구 막 외면에 위치하고 있으며 p-nitrophenylphosphate에 대한 Km치는 0.11 mM 이었다. 본 효소는 그 활성에 $Mg^{2+}$ 등 2가 금속 ion을 요구치 아니하였으며, fluoride는 이 효소를 상경적으로 억제하였고 이 억제는 2가 금속 ion을 요구치 않았다. 따라서 fluoride의 억제 작용은 metalofiuorophosphate 형성을 통해서라기 보다는 fluoride의 효소에 대한 직접적인 작용이라고 시사되었다. Acid phosphatase of the rabbit erythrocyte membrane was confirmed to be oriented to the outer surface of the cell membrane. The enzyme was competitively inhibited by fluoride ion when p-nitrophenylphosphate was the substrate, and this inhibition by fluoride occured in the presence or absence of divalent metal ions which were also not required for the enzyme activity. The inhibition by fluoride suggested that it is due to the direct actions of fluoride rather than through the formation of metalofiuorophosphate.
적혈구 막 Acid Phosphatase 에 관한 연구
지은정 ( Eun Chung Jhee ) 생화학분자생물학회 1974 BMB Reports Vol.7 No.2
Acid phosphatase of the rabbit erythrocyte membrane was confirmed to be oriented to the outer surface of the cell membrane. The enzyme was competitively inhibited by fluoride ion when p-nitrophenylphosphate was the substrate, and this inhibition by fluoride occurred in the presence. or absence of divalent metal ions which were also not required for the enzyme activity. The inhibition by fluoride suggested that it is due to the direct actions of fluoride rather than through the formation of metalofluorophosphate.
Phosphoadenosine Diphosphate Ribose의 닭 혈청에서의 대사
지은정 ( Eun Chung Jhee ) 생화학분자생물학회 1976 BMB Reports Vol.9 No.3
p-ADPR was prepared from NADP^+ by the action of NADP nucleosidase of rabbit erythrocyte membrane in the presence of urea and its metabolic fate was elucidated. The experimental evidence that p-ADPR is metabolized to AMP and ribose-5-phosphate via ADPR by the sequential actions of alkaline phosphatase and ADPR pyrophosphohydrolase is as follows: 1) A specific enzyme responsible for the direct hydrolysis of pyrophosphate linkage of p-ADPR could not be isolated in chicken serum, even though the hydrolytic activity for p-ADPR was high. 2) Hydrolytic cleavage of p-ADPR was strongly reduced in the presence of inorganic phosphate, an inhibitor of phosphata=_e, while that of ADPR was not affected. 3) Enzymatic production of inorganic phosphate from p-ADPR was much greater than that of ribose-5-phosphate. 4) ADPR, AMP and ribose-5-phosphate were detected as the end products of p-ADPR by chromato-graphy.
赤血球의 Methylene Blue攝取 와 Pentose 形成能에 미치는 高溫保管의 影響
池垠政 全北大學校 1975 論文集 Vol.17 No.-
Human erythrocytes were incubated at 30°for various time intervals up to 7 days in Na-phosphate buffer(pH 7.4) or acid-citrate-dextrose(ACD) solution. During incubation, the uptake of methylene blue and the formation of pentose from glucose or inosine were assayed to observe the effect of storage at high temperature(30°) on the glucose metabolism of erythrocytes. During incubation of red cells at 30°in Na-phosphate buffer, the methylene blue uptake in the presence of glucose decreased rapidly, and the formation of pentose from glucose also decreased gradually. The concentration of pentose in the erythrocytes was not correlated to the activity in converting pentose to glucose-6-phosphate. In contrast when inosine was added in place of glucose to red cell suspension, the methylene blue uptake and pentose formation remained unchanged during the incubation, and also the activity of converting pentose to glucose-6-phosphate was well correlated to the pentose concentration in the cells. The erythrocytes incubated at 30°in ACD solution showed the similar changes in methylene blue uptake, penotse formation in the presence of glucose, and the converting activity of pentose to glucose-6-phosphate, however, when inosine was substrate, methylene blue uptake, pentose formation, and the converting activity of pentose to glucose-6-phosphate decreased gradually during incubation. These results suggest that the incubation of erythrocytes at 30°causes the rapid depletion of adenosine triphosphate(ATP) in the erythrocytes, leading to the decreased activity in nucleoside phosphorylase and in the conversion of triose phosphate to glucose-6-phosphate in Embden-Meyerhof Pathway. It is also suggested that the activity in the formation of triose phosphate from pentose in pentose phosphate pathway and in the later half of Embden-Meyerhof Pathway (triose phosphate→lactate) is relatively well preserved during the incubation of red cells at 30°up to 7 days.
Studies on NAD Glycopydrolase of Rabbit Thymocytes
지은정,김우현,김형로 생화학분자생물학회 1985 BMB Reports Vol.11 No.4
Rabbit thymocytes were isolated from the thymus, and some properties of NAD Glycohy drolase (NADase) of thymocyte were investigated. This enzyme retained its maximal activity at pH 6.8 and its apparent Michaelis constant for NAD was 4 mM. Nicotinamide at a concentration of 6mM caused 50% inhibition of this enzyme activity while even high concentrations (20mM) of isunicotinic acid hydrazide (1NH) brought only 30% inhibition with the formatiun of INH analogue of NAD. The specific activity of thymocytes NADase was highest among the NADases of other rabbit tissues investigated such as speen, liver, brain, lung, erythrocytes and kindney. NADase activity both in intact and homogenate thymocytes was same, suggesting that this enzyme is an ectoenzyme.
白鼠 胃의 Alcohol Dehydrogenase에 關한 硏究
池垠政,李武三 전북대학교 의과학연구소 1978 全北醫大論文集 Vol.2 No.-
The enzymatic properties of rat stomach alcohol dehyrogenase was characterized in comparison to the liver alcohol dehydrogenase and the physiological role of this enzyme in the metabolism of ethanol was also studied. Stomach alcohol dehydrogenase was different from that of liver in Km for ethanol, substrate specificity, and temperature optimum. The optimal temperature of stomach enzyme was 55˚C, much higher than that of liver enzyme, while both of them attained the maximal activity at pH 11. The stomach enzyme had a stronger affinity to aromatic alcohols such as benzyl and furfuryl alcohol than ethanol. The Michaelis constant of stomach alcohol dehydrogenase for ethanol was 220mM, about 700 times higher than that of liver alcohol dehydrogenase, whereas they had comparable affinity to NAD. NAD concentrations in the stomach and liver were much less than th Km values for NAD of alcohol dehydrogenase from those organs, suggesting that NAD is an important regulatory factor in the metablism of ethanol. The constant rate of ethanol clearance regardless of its concentration in blood together with the limited content of NAD and the low total activity of ADH in the stomach indicates that alcohol dehydrogenase of rat stomach cannot be expected to play a significant role in the metabolism of ethanol.