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- W2039732092 abstract "We have separated the extracellular cyclic AMP phosphodiesterase produced by Dictyostelium discoideum into three activities (A, B and C) which differ in both molecular weight and isoelectric point. They are apparently composed of different associations of two glycoprotein subunits with molecular weights of 50 000 and 52 000 (p50 and p52, respectively). Phosphodiesterase A contains p50 only, B contains approximately equal amounts of p50 and p52 and C contains approximately twice as much p52 as p50. The p50 polypeptides associated with the three forms of the enzyme appear to be identical, as do the p52 polypeptides associated with B and C. p50 and p52 are distinct polypeptides but they contain a number of common peptides, establishing a relationship between the two. p52 contains approx. 25% more carbohydrate than p50. Finally, homogeneously pure phosphodiesterase A (p50 alone) was used to raise antiserum which was shown to immunoprecipitate not only phosphodiesterase A activity but also phosphodiesterase B and phosphodiesterase C. The major immunoprecipitated polypeptides were p50 and p52." @default.
- W2039732092 created "2016-06-24" @default.
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- W2039732092 date "1983-12-01" @default.
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- W2039732092 title "Characterization of the cyclic AMP phosphodiesterase activity secreted during development of Dictyostelium discoideum" @default.
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- W2039732092 doi "https://doi.org/10.1016/0167-4838(83)90233-9" @default.
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