ヒト胃粘膜ガラクトース転移酵素活性の研究

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書誌事項

タイトル別名
  • A study on the galactosyltransferase activity of human gastric mucosa
  • 第一編 オボムコイドを基質とした測定法の基礎的検討
  • Part 1. Assay conditions with ovomucoid as a substrate
公開日
1987
DOI
  • 10.4044/joma1947.99.5-6_657
公開者
岡山医学会

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説明

The conditions assaying for UDP-galactosyltransferase in human gastric mucosa was studied. Ovomucoid without any pretreatment was employed as a substrate. The optimal pH was 6.8. Manganese, 2-mercaptoethanol and Triton X-100 were required for maximum enzyme activity. In the standard assay; 20 μl of enzyme solution was added to 30 μl of 50 mM MES buffer containing 5 mM 2-mercaptoethanol, 15 mM MnCl2, 9.9mg protein/ml ovomucoid, 0.3 mM UDP-galactose, 1.7 μCi/ml UDP-[3H]-galactose and 1.5 mg/ml Triton X-100, and incubation was carried out at 37°C for 20 min. [3H]-labelled ovomucoid was the only radioreactive reaction product detected. All galactose residue incorporated was liberated by β-galactosidase but not by α-galactosidase.

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