ラット小腸平滑筋におけるPhosphatidylethanolamineの水解に関する研究
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Studies on enzymatic hydrolysis of phosphatidylethanolamine in rat small intestinal smooth muscle were carried out in comparison with that in the small intestinal mucosa. The hydrolytic activity was measured by incubation in 0.1 M Tris-maleate buffer solution containing 700×g homogenate of the tissue as the enzyme source and 32P-phosphatidylethanolamine isolated from rat small intestine as the substrate. Occurrence of hydrolytic activity of phosphatidylethanolamine was clearly demonstrated in the small intestinal smooth muscle as well as in the mucosa, although the activity of the former was as low as 45% of that of the latter. Then the additional investigations were followed. Optimum pH was found to be at 7.2. The results obtained by preincubation at different temperatures showed that the enzyme (s) related to the hydrolysis of phosphatidylethanolamine were heat-labile and the hydrolytic activity on the lysocompounds was more sensitive to the increase of temperature than that of the release of fatty acid from the original phospholipids. An addition of deoxycholate resulted in lowering of the hydrolytic activity. An addition of Ca++ accelerated the hydrolysis markedly, while the effect of Mg++ on the hydrolysis was slight. In comparison to the hydrolysis in three types of phosphatidylethanolamine, namely diacyl-, alkenyl- acyl- and alkyl-acyl-type, the hydrolysis of diacyl-type was more significant than that of the latter two types. The extent of the hydrolysis between alkenyl-acyl and alkyl-acyl-type was almost similar.
- 1977-08-01
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