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KMID : 0377219830080010011
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Medical Journal of Chosun Univercity
1983 Volume.8 No. 1 p.11 ~ p.18
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A Study on the Activity of Lactate Dehydrogenase IsoZymes in Erythrocytes of Phenylhydrazine-treated Rabbits
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金良均/Kim, Yang-Kyun
朴在允/車鍾希/高光三/李根培/Park, Jae-Yoon/Cha, Chong-Hee/Koh, Kwang-Sam/Lee, Keun-Bai
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Abstract
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A studv on erythrocytes during cytodifferentiation was carried out to clarify the general pattern of synthesis and breakdawn of lactate dehydrogenase (L-lactate : NAD oxido reductase, EC 1.1.1.27) isozymes in phenyl ydrazine treated domestic rabbits.
The rabbits were injected with phenylhydrazine on day 0,1 and 3 day and. at interyals, the blood samples were taken by cardiac puncture, and the activity of lactate dehydrogenase in try throcytes was determined according to the method of Stolzenbach.
The results obtained were as follows :
1. Total activity of lactate dehydrogenase in normal erythrocytes was about 4.9 units. and the relative activity of cytosolic and mitochondriai lactate dehydrogenase isozymes was approximately 99% and 0.01%, respectively.
2. In phenylhydrazine-produced reticulocytosis, the total lactate dehydrogenase activity was maximal on 4th day, about 27 units, which is about five-fold higher han that of normal value.
3. The increase in total activity of lactat dehydrogenase during the induction of reticulocytiosis was due primarily to 5.6 fold increase in the cytosolic isozyme(Ks = 0.0863 ; Kd=0.0.031 ; t 1/2 = 223 = hrs). The ctivity pf mitochondrial isozyrne was found to remain almost unchanged.
4. The rates of constants following recovery from phenylhydrazine treatment were : Ks = 0. 0029 ; Kd = 0.0486 ; t I/2 =14hrs, for mitochondrial isozyme and Ks = 0. 1118 ; Kd = 0. 0233 ; t 1/2 = 29hrs for cytosolic isozyme.
5. The possible physiological role of lactate dehydrogenase isozymes in erythrocytes during reticulocytosis and maturation was discussed.
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