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- W2077921710 abstract "Abstract The unnatural amino alcohol, N-isopropylethanolamine, is incorporated into phospholipids of various membrane fractions of rat liver after it is injected intraperitoneally. When this base analog was incorporated into the phospholipids of plasma membranes, the activity of 5'-nucleotidase in cell-free homogenates and in purified plasma membranes decreased by approx. 20–50% of that in the control preparations. Arrhenius plots for 5'-nucleotidase in both the control and isopropylethanolamine-treated plasma membranes had break points at the same temperatures. The enzymes from both control and isopropylethanolamine-treated membranes had identical apparent Michaelis constants, but different maximum velocities. Removal of phospholipids from control and isopropylethanolamine-treated plasma membrane preparations by phospholipase C treatment did not affect their 5′-nucleotidase activities. In addition, incubation of control membranes in the presence of free isopropyl-ethanolamine (1–10 mM) did not alter the 5'-nucleotidase activity. Collectively, these data indicate the lowered 5'-nucleotidase activity in the isopropyl-ethanolamine-treated membranes is due to a decreased amount of the enzyme and cannot be explained by the modification of the phospholipids within the membrane where the enzyme resides. Three other membrane-bound enzyme activities (NADH:cytochrome c reductase (EC 1.6.99.3), NADPH:cytochrome c reductase (EC 1.6.2.4), and succinic acid dehydrogenase (EC 1.3.99.1)) were not affected by the isopropylethanolamine treatment." @default.
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- W2077921710 date "1978-10-01" @default.
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- W2077921710 title "Enzyme activities in lipid-modified membranes of rat livers" @default.
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- W2077921710 doi "https://doi.org/10.1016/0005-2760(78)90189-3" @default.
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