RESUMO
Human serum albumin (HSA) was shown to mediate oligoribonucleotide cleavage. Nonenzymatic glycation of HSA decreased the ribonuclease-like activity of the protein. According to (31)P NMR data, both native and glycated albumins induced hydrolysis of RNA molecule through 2',3'-cyclophosphate intermediates. A feasible mechanism of RNA hydrolysis by native albumin and its clinically relevant modification was discussed.
Assuntos
Oligorribonucleotídeos/química , Albumina Sérica/química , Bioquímica/métodos , Cromatografia por Troca Iônica/métodos , Humanos , Hidrólise , Ligantes , Espectroscopia de Ressonância Magnética , Modelos Químicos , Ácidos Nucleicos/química , Fosfatos/química , Ligação Proteica , RNA/química , Albumina Sérica/metabolismoRESUMO
Using affinity columns with immobilized poly(A), poly(G), poly(U), poly(C), and poly(A).poly(U) and poly(G) x poly(C) duplexes several polyribonucleotide-binding blood plasma proteins have been captured. Albumin and keratins K1 and K2e have been detected to bind polypurine tracts. The in vitro glycated albumin binds poly(A) and poly(G) more efficiently than the unmodified protein. The major polypyrimidine-binding blood plasma protein (28 kDa) can catalyze the hydrolysis of poly(U).
