Journal of Okayama Medical Association
Published by Okayama Medical Association

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Full-text articles are available 3 years after publication.

ヒト胃粘膜ガラクトース転移酵素活性の研究 第一編 オボムコイドを基質とした測定法の基礎的検討

香川 俊介 岡山大学第一内科学教室 ORCID Kaken ID publons researchmap
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抄録
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 MnCl(2), 9.9mg protein/ml ovomucoid, 0.3 mM UDP-galactose, 1.7 μCi/ml UDP-[(3)H]-galactose and 1.5 mg/ml Triton X-100, and incubation was carried out at 37℃ for 20 min. [(3)H]-labelled ovomucoid was the only radioreactive reaction product detected. All galactose residue incorporated was liberated by β-galactosidase but not by α-galactosidase.
キーワード
human gastric mucosa
glycoprotein
UDP-galactosyltransferase
ovomuciod
N-acetylglucosamine
ISSN
0030-1558
NCID
AN00032489