Abstract
Biosynthetically labelled C1q secreted by guinea pig peritoneal macrophages was analysed by sedimentation through sucrose gradients followed by SDS-PAGE. In addition to the haemolytically active C1q of mol. wt 460,000 Da a low mol. wt (LMW) form of C1q was identified which had no detectable affinity for Fc of aggregated immunoglobulin, but which retained the ability to associate with the C1r2s2-complex. This LMW-C1q was covalently associated with two additional polypeptides of mol. wt 46 and 50 kDa.
MeSH terms
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Animals
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Centrifugation, Density Gradient
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Complement Activating Enzymes / biosynthesis*
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Complement Activating Enzymes / immunology
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Complement Activating Enzymes / metabolism*
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Complement C1 / biosynthesis*
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Complement C1 / immunology
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Complement C1 / metabolism*
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Complement C1q
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Complement C1r
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Complement C1s / metabolism*
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Electrophoresis, Polyacrylamide Gel
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Female
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Guinea Pigs
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Hemolysis
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Immunoglobulin Fc Fragments / immunology*
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Macrophages / immunology*
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Male
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Molecular Weight
Substances
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Complement C1
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Immunoglobulin Fc Fragments
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Complement C1q
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Complement Activating Enzymes
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Complement C1r
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Complement C1s