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Purification of the ninth component of the bovine complement cascade

Eisenschenk, F.C.; Houle, J.J.; Hoffmann, E.M.

American Journal of Veterinary Research 53(4): 435-439

1992

ISSN/ISBN: 0002-9645
PMID: 1586009
Document Number: 392298
Conditions for purification of the ninth component of bovine complement (C9) were established. The conditions for binding and eluation 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 of polyacrylamide gel electrophoresis. Some preparations of bovine C9 migrated as 2 bands when partially reduced, but extensively reduced preparations had a single band.

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