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. 1980 Jul;40(3):417–424.

Stabilization of the classical pathway C3 convertase C42, by a factor F-42, isolated from serum of patients with systemic lupus erythematosus.

M R Daha, H M Hazevoet, L A Vanes, A Cats
PMCID: PMC1458054  PMID: 6903557

Abstract

Sera from sixteen patients with SLE were investigated for the presence of a factor which would conserve convertase activity on preformed EAClgp 4hu2hu for 30 min at 30 degrees in EDTA. Although such a factor could not be detected readily in the sera, chromatography on DE-52 cellulose yielded fractions appearing as three peaks in one patient and as two peaks in a second patient. These peaks were capable of conserving C42 activity and were designated as F-42. Purification of F-42 from the second peak eluting between 4 and 7 mS on DE-52 was obtained by SP-C50, S-300 and QAE-A50 chromatography. F-42 exhibited charge heterogeneity upon SP-C50 chromatography. On polyacrylamide gel electrophoresis the final material migrated as one band, which coincided with the position of F-42 activity upon eluation from a parallel gel. F-42 had an apparent molecular weight of 150,000 and reacted with anti-IgG in Ouchterlony analysis. Sepharose-bound anti-IgG was capable of neutralizing F-42 activity. The purified material was shown to prolong the half-life (T 1/2) of performed cell-bound C42 in GVB-EDTA at 30 degrees from 5 to 80 min.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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