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KMID : 0366219830180010003
Korean Journal of Hematology
1983 Volume.18 No. 1 p.3 ~ p.11
Identification of the C1q Inhibitor in Dog Sera
±è»óÈ£(ÐÝßÓûÇ)/Sang Ho Kim
Abstract
During the purification and isolation of dog C1q by the euglebulin
precipitation method, some IgM and IgG remain closely associated with the
C1q throughout the isolation procedure, even when the C1q
was additionally purified by adsorption to and elution from Concanavalin A-Sepharose.
An inhibitor of C1q hemolytic activity was present amidst the proteins
that failed to adhere to Con A-Sepharose.
During gel filtration on Sepharose 6 B in 6 M urea, the C1q inhibitor
migrated with fraction rich in IgM.
But dog IgM purified by affinity chromatography from the fractions rich in
C1q inhibitor did not inhibit the hemolytic activity of dog
C1q. An antiserum raised against partially purified dog C1q
demonstrated two components in the Con A effluent of partially purified
C1q that were neither IgM nor IgG. When analyzed by SDS-PAGE under
reducing conditions these components migrated at 100 K Conceivably this may pertain to
the C1q inhibitor.
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