ラット胃粘膜ガラクトース転移酵素活性の研究第1編測定法と絶食負荷について

概要

論文の詳細を見る
A method to measure the activity of an enzyme catalyzing sugar chains which are abundant in O-glycosidic linkage was studied using UDP-galactosyl transferase (UDP-Gal-T) found in the gastric mucosa of rat and asialo-bovine-submaxillar-mucin (ASBSM) as a substrate. The optimum pH for the measurement was 7.5, Mn(++) was required, and about twice as much Triton X-100 was needed as when asialo-agalacto-fetuin (ASGF) was used as the substrate. The activity of UDP-Gal-T was measured simultaneously in a group of rats receiving food and a group fasted for 24 hours, using ASGF and ASBSM as substrates. With ASGF no significant difference was seen in either the glandular corpus or the pylorus, while with ASBSM, the activity decreased significantly (p<0.05) in the glandular corpus, though no significant difference was seen in the pylorus.
1986-06-30