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Canine Immunoglobulins

I. Evidence for Six Immunoglobulin Classes¹

Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, New York

Abstract

Structural and electrophoretic heterogeneity of immunoglobulins has been well documented in several species including man (1–3), guinea pig (4), horse (5, 6) and mouse (7, 8). In all these species antibodies of low molecular weight, 6.6S G, and high molecular weight, 18S M, have been identified. In addition, a third major class of immunoglobulin, A, has been described in human, equine and murine sera characterized by a fast electrophoretic mobility, and a sedimentation coefficient of 6.5S to 7S with higher molecular weight polymeric forms frequently detectable. These three major classes of immunoglobulins exhibit not only differences in physicochemical properties but striking differences in biologic activity as well. Furthermore, subclasses of G have also been described in human beings, horses, guinea pigs and mice exhibiting differences in biologic behavior. Additional immunoglobulin classes have been documented in human sera (D) (9, 10) and equine sera (10S₁) (5) which as yet appear unique for these species.

Footnotes

Supported by Grants AM 02443, AI 02349 and 2 T1 AI 28 from the National Institutes of Health.

² Recipient, Post-Doctoral Fellowship Award from The Arthritis Foundation. Present address: National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland.

³ Recipient, Research Career Award from the National Institutes of Health.