Direct photoaffinity labeling by nucleotides of the apparent catalytic site on the heavy chains of smooth muscle and Acanthamoeba myosins.
作者： H. Maruta , E.D. Korn
DOI: 10.1016/S0021-9258(19)70165-3
关键词: Subtilisin 、 Skeletal muscle 、 Biochemistry 、 Myosin light-chain kinase 、 Trypsin 、 Photoaffinity labeling 、 Chemistry 、 Nucleotide 、 Proteolysis 、 Myosin
摘要: The heavy chains of Acanthamoeba myosins. IA, IB and II, turkey gizzard myosin, rabbit skeletal muscle myosin subfragment-1 were specifically labeled by radioactive ATP, ADP, UTP, each which is a substrate or product ATPase activity, when irradiated with UV light at 0 degrees C. With as much 0.45 mol/mol IA chain 1 was incorporated. Evidence that the ligands associated catalytic site included observations reaction occurred only nucleotides are substrates products activity; blocked pyrophosphate an inhibitor ATP bound ADP; label probably restricted to single peptide following limited subtilisin proteolysis extensive cleavage CNBr trypsin chain.
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