STRUCTURE AND MECHANISM OF ACTION OF CYCLIC AMP-DEPENDENT PROTEIN KINASE
作者： Evgenii S. Severin , Lidia P. Sashchenko , Sergei N. Kochetkov , Nikita N. Gulyaev , Sergei N. Kurochkin
DOI: 10.1016/B978-0-08-023178-5.50014-8
关键词:
摘要: Publisher Summary This chapter discusses the structure and mechanism of action cyclic AMP-dependent protein kinase. In a study described in chapter, pig brain was chosen as source The holoenzyme isolated by method that includes steps such homogenization, acidic precipitation, chromatography on DEAE-Sephadex A 50, ammonium sulfate hydroxyapatite, gel filtration Sephadex G-200, DEAE-cellulose. existence negative charge cyclophosphate group is indispensable requirement. All analogs had no did not practically bind to enzyme. At same time, displacement from ionized carboxyl affect markedly binding analog. Modification heterocyclic base general leads decrease affinity modification position 8 being less essential than or substitution exo-amino group. It can be assumed specificity AMP- GMP-dependent kinases dependent nature amino-acid residues active sites interact with purine near 6.
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