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KMID : 0377519780030010043
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Chung-Ang Journal of Medicine
1978 Volume.3 No. 1 p.43 ~ p.52
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Studies on Aspartate and Alanine Transaminase in Human Term Placenta
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Nam Tai-Woo
Lee Hi-Sung
Lee Keun-Bai
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Abstract
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Activity of aspartate aminotransferase (GOT, L-aspartate 2-oxoglutarate aminotransferase : EC 2. 6. 1. 1) and alanine aminotransferase (GOT, L-alanine 2-oxoglutarate aminotransferase : EC 2. 6. 1. 2) of cytosolic and mitochondrial fractions from human placenta was studied. Isozyme patterns of these enzymes was also examined by using DEAE-cellulose column chromatography. The results obtained were as follows : 1. The activity of aspartate and alanine aminotransferase was about 2,150 units and 65 units per 1 g of fresh tissue, respectively. 2. The activity of mitochondrial aspartate aminotransferase was lower and accounts for about 5 per cent of the total activity found in the homogenate : most of the activity (about 95 per cent) was present in the cytosolic fraction. About 9 per cent of the total alanine aminotransferase activity was found in the mitochondrial fraction, about 91 per cent in the cytosolic fraction. 3. Aspartate aminotransferase from cytosolic fraction was separated by DEAE-cellulose column chromatography into three types of isozymes. The mitochondrial fraction also contained three types of isozymes. 4. Whereas alanine aminotransferase from cytosolic fraction gave only one active peak on DEAE-cellulose column chromatogram.
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