Effect of polynucleotides and a basic protein on the condensation of phenylalanyl adenylate.
The effect of polyuridylate and of histone on the oligomerization of phenylalanyl adenylate was tested. Polyuridylate which pairs with adenine under suitable conditions showed no effect. Histone increased the rate of the polymerization whereas a neutral protein, albumin, had no effect. Simultaneous presence of nucleotides diminished the effect of histone. The implication of these results on the prebiotic polypeptide formation is discussed.
D000249:Adenosine Monophosphate / Q000031:analogs & derivatives*; D000818:Animals; D002417:Cattle; D002625:Chemistry, Organic; D006657:Histones; D007700:Kinetics; D055601:Organic Chemistry Phenomena; D010649:Phenylalanine; D011072:Poly U; D012710:Serum Albumin, Bovine; D013950:Thymus Gland
D006657:Histones; D011072:Poly U; D012710:Serum Albumin, Bovine; C026617:phenylalanyl adenylate; D000249:Adenosine Monophosphate; D010649:Phenylalanine