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- W2008906997 abstract "Abstract Enzyme activity of immunoprecipitated plasma membrane antigens was quantitatively investigated employing various phosphodiesterase substrates. The highest activity was found with thymidine 5′-monophospho-p-nitrophenyl ester at pH 9.5–10.0 thus characterizing the enzyme(s) as alkaline phosphodiesterase I (EC 3.1.4.1). Furthermore, inhibition studies of this activity with different nucleotide pyrophosphatase substrates demonstrated a dual specificity against phosphodiester and nucleotide pyrophosphate bonds. Zymogram staining for alkaline phosphodiesterase activity of plasma membrane antigens separated in crossed immunoelectrophoresis revealed three different antigens posessing this activity. By inclusion of ATP, ADP or AMP into the staining medium, the alkaline phosphodiesterase activity of one of the antigens was completely inhibited while the staining of the two others was unaffected. All three phosphodiesterase-active antigens were found to be identical with some plasma membrane antigens previously characterized as multienzyme complexes. Thus, all of these antigens also exhibited nucleoside di- and triphosphatase activity; two of them also showed an NADH-oxidizing function, and one was in addition arylamidase-active. Affinity chromatography of plasma membrane extracts on columns of concanavalin A-Sepharose as well as analysis in fused rocket immunoelectrophoresis using concanavalin A-Sepharose containing intermediate gels revealed that all three alkaline phosphodiesterase-active antigens bound to the lectin, thus demonstrating the presence of carbohydrate in these antigens." @default.
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- W2008906997 date "1980-05-01" @default.
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- W2008906997 title "Alkaline phosphodiesterase-active antigens in plasma membranes of rat liver" @default.
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- W2008906997 doi "https://doi.org/10.1016/0005-2736(80)90008-5" @default.
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