title: Human serum albumin as a catalyst of RNA cleavage: N-homocysteinylation and N-phosphorylation by oligonucleotide affinity reagent alter the reactivity of the protein.
abstract: Kinetic parameters for the cleavage of UpA site in an oligonucleotide in the presence of human serum albumin (HSA) or one of its clinically relevant modification were measured. The RNA-hydrolyzing activity of HSA was decreased by its nonenzymatic N-homocysteinylation. According to (31)P NMR data, Lys and Tyr residues were the labeling targets when a phosphorylating analog of oligoribonucleotide substrate was employed. The site of tyrosine modification was slowly dephosphorylated. Lys-directed affinity labeling suppressed oligonucleotide cleavage indicating that lysines took part in the reaction.
authors.affiliation: Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, 8 Lavrentyev Avenue, 630090 Novosibirsk, Russia.
authors.forename: Yuliya V
authors.initials: YV
authors.lastname: Gerasimova
authors.forename: Dmitry D
authors.initials: DD
authors.lastname: Knorre
authors.forename: Makhmut M
authors.initials: MM
authors.lastname: Shakirov
authors.forename: Tatyana S
authors.initials: TS
authors.lastname: Godovikova
mesh_terms: D002384:Catalysis; D004591:Electrophoresis, Polyacrylamide Gel; D006710:Homocysteine / Q000737:chemistry*; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D008239:Lysine / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D015233:Models, Statistical; D009841:Oligonucleotides / Q000737:chemistry; D010766:Phosphorylation; D012313:RNA / Q000737:chemistry*; D012709:Serum Albumin / Q000737:chemistry*; D014443:Tyrosine / Q000737:chemistry
chemical_list: D009841:Oligonucleotides; D012709:Serum Albumin; D006710:Homocysteine; D014443:Tyrosine; D012313:RNA; D008239:Lysine