ISOLATION AND PARTIAL CHARACTERIZATION OF LYMPHOCYTE SURFACE IMMUNOGLOBULINS

doi:10.1084/jem.135.4.956

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ARTICLE

ISOLATION AND PARTIAL CHARACTERIZATION OF LYMPHOCYTE SURFACE IMMUNOGLOBULINS

John J. Marchalonis ¹, Robert E. Cone ¹, and John L. Atwell ¹

¹ From The Walter and Eliza Hall Institute of Medical Research, The Royal Melbourne Hospital, Victoria, Australia

Immunoglobulins were isolated from the surfaces of lymphocytesfrom a variety of lymphocyte populations including murine andhuman thymus lymphocytes and murine spleen and thoracic ductlymphocytes. Cell surface proteins were labeled with iodide-¹²⁵Iby lactoperoxidase-catalyzed iodination, and recovered in solutioneither by solubilization in dissociating solvents or activemetabolic release. Immunoglobulins were identified and isolatedby immunological coprecipitation. The polypeptide chain structureof immunoglobulins isolated from lymphocyte surfaces was analyzedby polyacrylamide gel electrophoresis of reduced, alkylatedsamples in acid urea. Human and murine thymus lymphocytes possessedonly IgM immunoglobulin on their surfaces. This protein containedlight chains and µ-type heavy chains and was characterizedby a molecular weight of approximately 200,000. Murine spleniclymphocytes from CBA x C57 animals and congenitally athymic(nu/nu) mice possessed both IgM and IgG on their surfaces. Theratio of µ-chain to $gamma$ -chain was about 3/1. The presenceof IgM on thymus lymphocytes probably does not reflect tracecontamination by B lymphocytes because comparable quantitiesof IgM were isolated from both cell populations. Metabolic turnoverdata suggest that this immunoglobulin is synthesized by thecell population studied.

These results provide direct evidencefor the presence of immunoglobulins composed of light and heavypolypeptide chains on the surfaces of lymphocytes of all classes.

Submitted on December 20, 1971

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