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Phylogeny of Immunoglobulin Structure and Function

VI. 17S, 7.5S and 5.7S anti-DNP of the Turtle, Pseudamys Scripta

From the Department of Microbiology and Immunology, Tulane University School of Medicine, New Orleans, Louisiana 70112, and Department of Immunology and Medical Microbiology, University of Florida College of Medicine, Gainesville, Florida 32601

Abstract

Three different sizes of immunoglobulins containing anti-dinitrophenyl activity were isolated from turtles immunized with dinitrophenyl bovine globulin. The sedimentation coefficients of the three immunoglobulins were 17S, 7.5S and 5.7S and their molecular weights were 850,000, 180,000 and 120,000, respectively. The 17S immunoglobulin was similar to IgM and was composed of five subunits each with a molecular weight of 170,000. The heavy and light chain molecular weights were 70,000 and 22,500, respectively. The 7.5S molecule had H chains of 67,500 and L chains. The 5.7S molecule had H chains of 35,000 and L chains. Partial reduction of the 5.7S molecule resulted in the formation of half molecules of 61,000. Antigenic analyses suggested that the 5.7S molecule may be a fragment of the 7.5S molecule. Neither the 7.5S H chains nor the 5.7S H chains cross-reacted with the 17S H chains. These findings are discussed in relationship with the phylogeny in immunoglobulin structure and function.

Footnotes

¹ Supported by National Science Foundation Grant GB-31001 and United States Public Health Service General Research Grant 5501-FR-05377-09.

² Supported by National Science Foundation Grant GB-8632.