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The Purification and Reactivity of the First Component of Complement from Guinea Pig, Human and Canine Sera¹

Laboratories of Microbiology, Howard Hughes Medical Institute, 1550 Northwest 10th Avenue, Miami, Florida 33136

Abstract

A simple procedure for separation and purification of the first component of guinea pig complement is described. The product has high specific reactivity, low protein content and minimal content of other complement components. The formation of EAC1 using sheep erythrocytes sensitized with purified IgG was greater at 0°C than at 37°C. In contrast, the formation of EAC1 using sheep erythrocytes sensitized with IgM proceeded more effectively at 37°C than at 0°C.

Preliminary results are presented on measurements of C1 by immune adherence as well as by immune hemolysis. Estimates of the number of molecules that are required for a 50% endpoint in each of these two reactions were 2 and 10 molecules per erythrocyte, respectively.

Certain problems concerned with the exact definition of the molecular weight of C1 in native serum are discussed.

Footnotes

¹ The components of complement are now designated by numbers according to criteria outlined by one of us (R.A.N.) at the Brugge Colloquium on Protides of Biological Fluids in May 1967 as well as recommendations of a panel held under the auspices of the World Health Organization at the same meeting. In brief, the new nomenclature represents the sequential reactivity of nine components as C1,4,2,3,5,6,7,8,9, which originally corresponded to C'1,4,2,3c,3b,3e,3f,3a,3b.

² Visiting Investigator from University of Tokyo, School of Medicine, Department of Serology. Present address: National Cancer Center Research Institute, Tsukiji 5-1, Tokyo, Japan.