Physico-chemical characterization of hamster interferon.
The glycoprotein nature of Syrian hamster interferon was tested on several immobilized lectins. The specific retention of a small portion (20%) of interferon activity was observed only on concanavalin A-agarose; Component I of the interferon (not retained) has an apparent molecular weight of 23,500 whereas Component II (retained) is larger, 31,500. The apparent hydrophobicity of Syrian hamster interferon was probed by its chromatography on: (a) straight chain hydrocarbons of varied length; (b) aromatic ligands (aminobenzene, benzylamine, beta-phenylethylamine, gamma-phenyl-propylamine); ligands listed in (a) and (b) were immobilized to cyanogen bromide-activated agarose (isourea linkage); and (c) phenyl-agarose (Phenyl-Sepharose CL-4B), an aromatic ligand immobilized via a 2-hydroxypropyl arm to the agarose (ether linkage).
D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D002472:Cell Transformation, Viral; D055598:Chemical Phenomena; D002621:Chemistry; D003208:Concanavalin A / Q000378:metabolism; D006224:Cricetinae; D006023:Glycoproteins; D006863:Hydrogen-Ion Concentration; D007372:Interferons / Q000302:isolation & purification; D007739:L Cells; D008647:Mesocricetus; D051379:Mice; D008970:Molecular Weight; D009522:Newcastle disease virus; D011817:Rabbits; D013045:Species Specificity
D006023:Glycoproteins; D003208:Concanavalin A; D007372:Interferons