The purification and characterization of interferons.
Significant advances have been made in the last four years on the purification of interferons. Components of several human and mouse interferons have been purified to homogeneity. Partial characterization of these molecules has been achieved (i.e. amino acid composition, analytical maps of radiolabelled tryptic peptides, and amino terminal amino acid sequence). In addition, preliminary evidence has been accumulated which implies that the carbohydrate portion of the molecules may play a significant role in species specificity of interferons. At present, with minute quantities of homogenous interferons available, limited structural information has been obtained. Using current production and purification schemes, sufficient material can be obtained for further amino acid sequence studies and examination of the carbohydrate portion of the molecules. Additional structural characterization of the interferon gene(s). Furthermore, as sequence homologies have been observed between human and mouse interferons, all new structural information will help to establish the interrelationships in the family of interferon proteins.
D000595:Amino Acid Sequence; D000818:Animals; D006023:Glycoproteins / Q000302:isolation & purification; D006801:Humans; D007372:Interferons / Q000302:isolation & purification*; D051379:Mice; D012995:Solubility; D013329:Structure-Activity Relationship
D006023:Glycoproteins; D007372:Interferons