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- W1454200749 abstract "Publisher Summary This chapter discusses the insulin-sensitive camp phosphodiesterase in rat adipose tissue. The activity of cAMP phosphodiesterase is determined from the rate of conversion of [ 3 H]cAMP into [ 3 H]AMP. [Phosphodiesterase is stimulated maximally when the insulin concentration is 1–3 nM. The stimulation observed in the cell homogenate is approximately 2-fold, and that detected in fraction P-2 is usually 2.5- to 3.0-fold. Both basal and plus-insulin activities are affected by contaminants in crude bacterial collagenase and crude bovine serum albumin. Crude bacterial collagenase contains an acidic proteinase that rapidly decomposes insulin. Therefore, cells prepared by the collagenase method must be washed carefully. The insulin-dependent stimulation of phosphodiesterase is energy dependent, but the addition of an energy source is usually unnecessary. If adipocytes are homogenized in the presence of 1 mM EDTA or dithiothreitol, little insulin effect is detectable. If cells are homogenized at pH 7.4, the basal enzyme activity is slightly elevated." @default.
- W1454200749 created "2016-06-24" @default.
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- W1454200749 date "1988-01-01" @default.
- W1454200749 modified "2023-10-14" @default.
- W1454200749 title "[68] Insulin-sensitive CAMP phosphodiesterase in rat adipose tissue" @default.
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- W1454200749 doi "https://doi.org/10.1016/0076-6879(88)59070-5" @default.
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