Affinity separation of polyribonucleotide-binding human blood proteins.
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).
Gerasimova
Yuliya V
YV
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, 8 Lavrentyev Ave., 630090 Novosibirsk, Russia.
Alekseyeva
Irina V
IV
Bogdanova
Tatyana G
TG
Erchenko
Irina A
IA
Kudryashova
Natalya V
NV
Chelobanov
Boris P
BP
Laktionov
Pavel P
PP
Alekseyev
Pavel V
PV
Godovikova
Tatyana S
TS
D001798:Blood Proteins / Q000737:chemistry* / Q000378:metabolism; D002846:Chromatography, Affinity; D006801:Humans; D011131:Polyribonucleotides / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism
D001798:Blood Proteins; D011131:Polyribonucleotides; D016601:RNA-Binding Proteins