cAMP-dependent protein kinase from Mucor rouxii: Physical evidence of a ternary complex holoenzyme-cAMP
作者： R.L. Pastori , N. Kerner , S. Moreno , S. Passeron
DOI: 10.1016/0006-291X(81)91310-3
关键词: Mucor rouxii 、 Biochemistry 、 Nucleotide 、 Protein kinase A 、 Histone 、 Biology 、 Protein subunit 、 Ternary complex 、 Half-life 、 Gel electrophoresis
摘要: Abstract Gel electrophoresis and sucrose density gradient centrifugation techniques permitted the visualization for first time of ternary complex formed by binding cAMP to Mucor rouxii cAMP-dependent protein kinase holoenzyme. The addition 0.5 M NaCl or histone plus ATP-Mg++, together with cAMP, dissociates holoenzyme into free regulatory (R) catalytic (C) subunits. At 4°C, bound is readily exchangeable unlabeled (half life 2.5 min), while nucleotide R subunit has a very slow exchange rate 210 min). amount approximately twice at saturation.
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