Electrophoretic Heterogeneity of the Polypeptide Chains of Human G-Myeloma Proteins
William D. Terry 1,
Parker A. Small Jr. 2, and
Ralph A. Reisfeld 3
1 Immunology Branch, National Cancer Institute, Bethesda, Maryland
2 Laboratory of Neurochemistry, National Institute of Mental Health
3 Laboratory of Immunology, National Institute of Allergy and Infectious Diseases
The light and heavy polypeptide chains derived from human Gmyeloma proteins are electrophoretically heterogeneous as judged by disc electrophoresis of the polypeptide chains in urea-acrylamide gels. Individual myeloma proteins contained as many as eight light-chain and nine heavy-chain components.