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Characterization of Three Feline Paraproteins¹

From the Department of Microbiology, Mount Sinai School of Medicine of the City University of New York, 10 East 102nd Street, New York, New York 10029 and the Animal Medical Center, 510 East 62nd Street, New York, New York 10021

Abstract

Serum protein electrophoretic studies on three cats, two with lymphosarcoma and one with multiple myeloma, revealed M components in the region. These proteins were isolated by zone electrophoresis and were characterized immunologically, physically and chemically. Antisera to two feline isolates demonstrated individual antigenic specificity. All three proteins were classified as G lambda immunoglobulins on the basis of cross-reactivities with human antisera. Cross-reactions were also documented between each of the feline proteins and previously studied canine light chains and intact human G proteins. By analytical ultracentrifugation these feline immunoglobulins had Svedberg constants of approximately 6.8S. Molecular weight determinations of the intact G proteins by SDS acrylamide gel analysis indicated an average m.w. of 154,000. The amino terminal amino acid residue of one of the feline heavy chains was glutamic acid and that of another aspartic acid. Thus these chains could be partially sequenced by an automatic protein sequencer. Comparison of the results with sequences of human V_HIII heavy chains showed a striking sequence homology between the two species.

Footnotes

¹ Aided by grants from the National Science Foundation (GB 17046), the United States Public Health Service (AI 09810), and a Grant-in-Aid from the New York Heart Association to J. M. K. and J. D. C., and by funds from Ms. Doris Duke to A. I. H.

² J. M. K. is an Established Investigator of the American Heart Association.

³ J. D. C. is the recipient of NIH Career Development Award 6-K4-GM-35, 190-01.