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The Journal of Immunology, 1963, 90: 238-245.
Copyright © 1963 by The American Association of Immunologists, Inc.

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Antiglobulins in Normal Serum

I. Characterization of Two Antiglobulins in Normal Rabbit Sera1

R. Glenn Watson2 and Nancy M. Collins3

From the Department of Microbiology and Immunology, Bowman Gray School of Medicine, Winston-Salem, North Carolina

Abstract

The Waaler-Rose activity previously noted in normal rabbit sera was studied. The factor responsible for this activity was found in all normal rabbit sera tested in titers of 1:64 to 1:2048. This factor was primarily localized in the water-soluble fraction of rabbit serum, was heat-stable at 56°C, and could be absorbed from rabbit serum with sheep erythrocyte stroma highly sensitized with rabbit hemolysin. No detectable amount of the Waaler-Rose factor could be removed from the serum by absorption with latex particles coated with human Cohn Fraction II. The Waaler-Rose factor in rabbit sera was differentiated from the Forssman heterophile antibody and the rheumatoid factors and was not associated with conglutinin activity.

A latex-fixation factor was demonstrable in all normal rabbit sera tested in titers of 1:20 to 1:512. This factor differed from the rabbit Waaler-Rose factor in that it was primarily confined to the water-insoluble fraction of the sera and was completely inactivated when the sera were heated at 56°C for 14 min. The latexfixation factor could be completely absorbed from rabbit sera by latex particles coated with human Cohn Fraction II. However, the absorption of rabbit sera with sheep erythrocyte stroma highly sensitized with rabbit hemolysin did not remove all of this factor but did remove about 75% of it. The latex-fixation factor in rabbit sera was differentiated from the Forssman heterophile antibody and the rheumatoid factors and was not associated with conglutinin activity. The addition of small amounts of normal human serum to rabbit serum containing high titers of latex-fixation activity caused inhibition of latex-fixation activity. The inhibitory substance in human serum responsible for the inhibition could be inactivated by heating the serum at 56°C for 30 min.

Footnotes

1 This study was supported by grants from the North Carolina Heart Association and the United Medical Research Foundation of North Carolina.

2 Instructor of Microbiology and Immunology, Department of Microbiology and Immunology, Bowman Gray School of Medicine of Wake Forest College, Winston-Salem, North Carolina.

3 Cardiovascular Graduate Trainee, USPHS Grant HTS-5392, June 1960–July 1961. Medical Student, Bowman Gray School of Medicine of Wake Forest College, Winston-Salem, N. C.







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