title: Purification of the ninth component of the bovine complement cascade.
abstract: Conditions for purification of the ninth component of bovine complement (C9) were established. The conditions for binding and elution from diethylaminoethyl cellulose and hydroxylapatite were different than for human C9. Serum albumin, a frequent contaminant of bovine C9 preparations, was removed by chromatography on reactive-red agarose. The calculated molecular weight of bovine C9 was 66,000, and reduction with 2-mercaptoethanol affected its migration on polyacrylamide gel electrophoresis. Some preparations of bovine C9 migrated as 2 bands when partially reduced, but extensively reduced preparations had a single band.
authors.affiliation: Department of Microbiology and Cell Science, University of Florida, Gainesville 32611.
authors.forename: F C
authors.initials: FC
authors.lastname: Eisenschenk
authors.forename: J J
authors.initials: JJ
authors.lastname: Houle
authors.forename: E M
authors.initials: EM
authors.lastname: Hoffmann
mesh_terms: D000818:Animals; D002417:Cattle / Q000097:blood / Q000276:immunology*; D011232:Chemical Precipitation; D002850:Chromatography, Gel; D003186:Complement C9 / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel
chemical_list: D003186:Complement C9