Isolation and characterization of Clq, Clr and Cls of human serum.

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Abstract
Clq, Clr and Cls, subcomponents of the first component of complement, have been isolated from human serum in highly purified form by DEAE-Sephacel chromatography and gel filtration through Sepharose 6B and Bio-Gel A 1.5m, and by dialysis against buffers of various ionic strengths. The methods gave excellent reproducibility and recovery. Average yields corresponded to about 16mg, 6mg and 3mg per liter of serum for Clq, Cls and Clr respectively.The preparations were analyzed by Tris-glycine buffer slab gel electrophoresis, isoelectric focusing gel electrophoresis, and circular dichroism spectra. Approximate molecular weights of activated Clr was 98, 000 and that of Cls was 88, 000.Analysis by isoelectric gel electrophoresis of Clr and Cls revealed some heterogeneity of isoelectric points. Analysis of circular dichroism spectra of these components showed that Cls mainly had a random coil structure and Clr had substantial amounts of β-structure; also, activated and unactivated forms showed identical spectra. Clr and Cls are activated by very similar mechanisms, but are distinguished by differences of molecular weight, isoelectric point and circular dichroism spectra.

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