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Science 27 May 1966:
Vol. 152. no. 3726, pp. 1253 - 1254
DOI: 10.1126/science.152.3726.1253
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Articles

Electrophoretic Heterogeneity of Polypeptide Chains of Specific Antibodies

Ralph A. Reisfeld 1 and Parker A. Small Jr. 2

1 Laboratory of Immunology, National Institute of Allergy and Infectiouis Diseases, Bethesda, Maryland 20014
2 Laborotarvy of Immunology, National Institute of Mental Health

Heavy and light polypeptide chains isolated from different specific antibodies to haptens and from ggrG-immunoglobulin of normal rabbits have been resolved into distinct, multiple components by disc electrophoresis in polyacrylamide gels in the presence of urea. In spite of the resolution of these chains into multiple bands, different specific antibodies and normal rabbit ggrG-immunoglobulin were indistinguishable from each other by this method.


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Light Chain Evolution.
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Heterogeneity of Rabbit Light-Polypeptide Chains.
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Electrophoretic Heterogeneity of the Polypeptide Chains of Human G-Myeloma Proteins.
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Science 152, 1628-1630
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Science. ISSN 0036-8075 (print), 1095-9203 (online)