Binding of 5,5'-bis[8-(phenylamino)-1-naphthalenesulfonate] by the regulatory subunits of adenosine cyclic 3',5'-phosphate dependent protein kinase.
Binding of 5,5'-bis[8-(phenylamino)-1-naphthalenesulfonate] by the regulatory subunits of adenosine cyclic 3',5'-phosphate dependent protein kinase.
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腺苷环状 3,5-磷酸依赖性蛋白激酶的调节亚基与 5,5-双[8-(苯氨基)-1-萘磺酸] 的结合。
DOI：
10.1021/bi00265a029
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发表时间：
1982
期刊：
影响因子：
2.9
通讯作者：
Fischer,EH
中科院分区：
文献类型：
--
作者：
Bohnert,JL;Malencik,DA;Anderson,SR;Teller,D;Fischer,EH
Janice L. Bohnert, Dean A. Malencik, Sonia R. Anderson, David Teller, and Edmond H. Fischer*摘要：与I型和II型腺苷环3’，5’-磷酸（cAMP）依赖性蛋白激酶（分别为R1和R11）的调控亚基结合，会显著增加5,5’-二[8-（苯胺）-1-萘磺酸][二（ANS）]的荧光和光学活性。包括特异性和非特异性相互作用。通过荧光和圆二色性的变化检测到，调节亚基与催化亚基或cAMP的结合会导致结合产物（ANS）的大部分解离。结果与公认的R1和R11的cAMP发现特性一致，R1与R11的两个异源结合位点表现出协同性。环鸟苷酸
Janice L. Bohnert, Dean A. Malencik, Sonia R. Anderson, David Teller, and Edmond H. Fischer* abstract: Binding to the regulatory subunits of types I and II adenosine cyclic 3', 5'-phosphate (cAMP) dependent protein kinase (R1 and R11, respectively) produces large distinctive increases in fluorescence and optical activityof 5, 5'-bis [8-(phenylamino)-1-naphthalenesulfonate][bis (ANS)]. Both specific and nonspecific interactions are involved. Association of the regulatory subunits with either the catalytic subunit or cAMP results in dissociation of a major portion of the bound bis (ANS) as detected by changes in fluorescence and circular dichroism. The results are consistent with the accepted cAMP finding properties of R1 and R11, showing cooperativity in the case of R1 and two heterologous binding sites for R11. cGMP