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福司可林与大鼠脑膜的高亲和力结合。

High-affinity binding of forskolin to rat brain membranes.

作者信息

Seamon K B, Daly J W

出版信息

Adv Cyclic Nucleotide Protein Phosphorylation Res. 1985;19:125-35.

PMID:3159185
Abstract

High-affinity forskolin binding sites in brain membranes have been identified that have structure-activity characteristics compatible with forskolin's site of action at the adenylate cyclase enzyme. It is proposed that these high-affinity binding sites are associated with an activated complex of the catalytic protein and the alpha s subunit. Quantitation of high-affinity forskolin binding sites may provide a direct measure of the amount of adenylate cyclase that has the potential to be regulated by stimulatory hormones and the Ns subunit.

摘要

已在脑膜中鉴定出高亲和力的福斯高林结合位点,其结构活性特征与福斯高林在腺苷酸环化酶上的作用位点相符。有人提出,这些高亲和力结合位点与催化蛋白和αs亚基的活化复合物相关。对高亲和力福斯高林结合位点的定量分析可能会直接测量出有潜力受刺激性激素和Ns亚基调节的腺苷酸环化酶的量。

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