Behavior of angiotensin octapeptides and dinitrophenyl-angiotensin during chromatography on polyacrylamide and dextran gels.

摘要: The behavior of the synthetic angiotensin II octapeptides (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe, molecular weight 1046, and its Asn1-Val5 congener, 1031) have been studied during gel chromatography on cross-linked polyacrylamide (Bio-Gel, P-2), dextran (Sephadex G-15). In case asparagine peptide adsorption was observed with both media. On marked at acid pH (0.05 N HCl), but 5.5 in 0.1 M pyridinium acetate compound could be separated from emerged between a larger (bacitracin, 1411) smaller molecules (pyridine—Cu2+ complex; Na+). asparagine1-angiotensin retarded due to not only also acetate, even more dilute alkali (0.01 NH4OH). Under none these conditions it possible ordinary separate amino acids or salts. sharp contrast, aspartic acid1-angiotensin excluded G-15 alkaline pH, two angiotensins were thus readily one another under conditions. Adsorption nearly abolished by 1 pyridine. separation is attributed greater negative charge acid1-argiotensin which results exclusion overcomes “aromatic” remainder molecule. The dinitrophenyl (DNP) derivative separable DNP-amino absolute methanol through an alkylated LH-20).