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)·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).

Graphical abstractAlbumin and keratins K1 and K2e are polypurine-binding blood plasma proteins. The in vitro glycated albumin binds poly(A) and poly(G) more efficiently than the unmodified protein. The 28 kDa polypyrimidine-binding blood plasma protein can catalyze the hydrolysis of poly(U).Figure optionsDownload full-size imageDownload as PowerPoint slide