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논문 기본 정보

자료유형
학술저널
저자정보
Min, Kyeong-Min (Department of Biology, Inha University) Bae, Young-Gi (Department of Biology, Inha University) Lee, Jong-Seob (Dept. Of Molecular Biology, Seoul National Univ.) Choi, Young-Hee (Department of Biology, Inha University) Cha, Young-Ryun (Department of Biology, Inha University) Cho, Sung-Ho (Department of Biology, Inha University)
저널정보
한국식물학회 식물학회지 식물학회지 제40권 제4호
발행연도
1997.1
수록면
234 - 239 (6page)

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Aminoalcoholphosphotransferase is the enzyme that catalyzes the synthesis of phosphatidylcholine and phosphatidylethanolamine from diacylglycerol using CDP-aminoalcohol such as CDP-choline and CDP-ethanolamine. To determine its cDNA structure from roots of Chinese cabbage, Brassica campestris L. ssp. pekinensis, degenerate primers were designed from the regions showing high amino acid homology between yeast CPT1 and soybean AAPT1 and used for PCR amplification of Chinese cabbage DNA. Chinese cabbage aminoalcoholphosphotransferase cDNA (AAPT) contains an open reading frame of 1,167 bp coding for a protein of 389 amino acids. It shared 81% identity and 94% similarity with soybean AAPT1 at the predicted amino acid level. Hydropathy profile analysis suggested that the predicted protein structure of Chinese cabbage aminoalcohophosphotransferase was very similar to the soybean enzyme, showing an overall hydrophobicity and having the same number of predicted transmembrane domains. Southern analysis indicated that there might be close isoforms of the enzyme. AAPT was expressed equally well in young shoots and roots.

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