RECONSTITUTION OF C1 IN NATIVE, PROENZYME FORM AND ITS USE IN A QUANTITATIVE C1 ACTIVATION TEST

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  • 1 January 1977
    • journal article
    • research article
    • Vol. 119  (5) , 1664-1667
Abstract
C1 [complement component 1] [human] was reconstituted in macromolecular proenzyme, non-activated form by incubation of highly purified C1q, C1r and 125I-C1s together in the presence of Ca. C1 reformed in this manner had an equimolar ratio of C1 subcomponents, as is found in serum, and sedimented in sucrose density gradients with the 16S rate characteristic of C1 in serum. Reconstituted C1 was activatable as shown by cleavage of the 87,000 dalton polypeptide chain of C1s into disulfide linked subunits of 59,000 and 28,000 daltons, respectively, after incubation with aggregated Ig[immunoglobulin]G. The extent of activation may be quantitated. Reformed activatable proenzyme C1 can be used to quantitatively assess the C1-activating properties of various substances in addition to its use in the analysis of the C1 activation process.

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