Further characterisation of a nucleic acid binding protein.
A glycoprotein which binds to nucleic acids has now been purified from Ustilago maydis until free from detectable deoxyribonuclease activity. It binds to a variety of substrates and in doing so, makes them soluble in dilute trichloroacetic acid. Physical studies suggest that it forms a variety of aggregates under low ionic strength, but at high ionic strength the monomer consists of a single polypeptide chain. Preliminary experiments have detected this novel binding activity in bacterial, fungal and mammalian cells.
D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification; D002417:Cattle; D004247:DNA; D006023:Glycoproteins / Q000302:isolation & purification; D007700:Kinetics; D008970:Molecular Weight; D012710:Serum Albumin, Bovine; D013045:Species Specificity; D013950:Thymus Gland; D014588:Ustilago / Q000032:analysis
D002352:Carrier Proteins; D006023:Glycoproteins; D012710:Serum Albumin, Bovine; D004247:DNA