Immunoaffinity purification of human complement component C9 using monoclonal antibodies.

B P Morgan; R A Daw; K Siddle; J P Luzio; A K Campbell

doi:10.1016/0022-1759(83)90434-9

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Immunoaffinity purification of human complement component C9 using monoclonal antibodies.

B P Morgan·R A Daw·K Siddle·J P Luzio·A K Campbell

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Abstract

Five monoclonal antibodies to human C9 were produced. Three of the antibodies had affinities from 1.6 to 3.1 X 10(9) M-1 and 2 were of lower affinity, 0.1 to 0.3 X 10(9) M-1. Four distinct antigenic sites on C9 were detected. The lowest affinity antibody was immobilised on Sepharose 4B and used to isolate C9 from human plasma. A 1200-fold purification was obtained with yield of 30-40%. The purified antigen maintained full cytolytic activity.

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Animals Antibodies, Monoclonal Antibody Affinity Binding, Competitive Complement C9 Electrophoresis, Polyacrylamide Gel Epitopes Guinea Pigs Humans Immunologic Techniques Isoelectric Focusing Mice Mice, Inbred BALB C Molecular Weight Rabbits Journal Article Research Support, Non-U.S. Gov't

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B P Morgan, R A Daw, K Siddle, J P Luzio, A K Campbell. 1983-11-25. Immunoaffinity purification of human complement component C9 using monoclonal antibodies.. https://doi.org/10.1016/0022-1759(83)90434-9

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