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From the Department of Pathology, University of Connecticut Health Center, School of Medicine, Farmington, Connecticut
Abstract
The chemotactic factor inactivator (CFI) has been isolated from whole human serum by a combination of techniques including salt precipitation, anionic exchange, and gel filtration chromatography. Two inactivators have been obtained, a
-globulin with a sedimentation velocity of approximately 7S and an
-globulin with a sedimentation velocity of approximately 4S. The former has a specificity for inactivation of the chemotactic activity associated with the C3 fragments, whereas the C5 chemotactic fragment is specifically inactivated by the
-globulin CFI. CFI in crude fractions of human serum is heat labile, time and temperature dependent for its activity, and pH dependent, expressing optimal activity at a pH range of 7.2 to 7.4.
Footnotes
1 This work was supported in part by National Institutes of Health Grants AI 09651 and AI 11526
2 G. T. is supported by Research Fellowship Grant Ti 63/4 from the Deutsche Forschungsgemeinschaft.
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