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The Effect on Antigenic Specificity of Changes in the Molecular Structure of Ribonuclease¹

From the Departments of Medicine and Biological Chemistry, Harvard Medical School and the Massachusetts General Hospital and the Biochemical Research Laboratory, Massachusetts General Hospital, Boston, Massachusetts

Abstract

Antigenic determinants of proteins apparently involve considerable lengths of the amino acid chain (1). Because of molecular folding, chemical groups on the surface of the molecule which might constitute an antibody binding site could be widely separated in the amino acid sequence. Changes in the three dimensional configuration of a protein, by altering the topography of such binding sites, should interfere with its immunologic specificity. The availability of a method for altering the spacial configuration of a purified protein, ribonuclease, to new and reasonably stable three dimensional structures without chemically changing the amino acid residues, offered an opportunity for testing this hypothesis.

Procedures which grossly denature proteins are known to result in a loss of antigenic specificity (2, 3), but the molecular changes caused by such methods are ill-defined. They probably involve covalent changes in a number of amino acid residues.

Footnotes

¹ This investigation was supported by Research Grant A 3564-0 from the National Institute of Arthritis and Metabolic Diseases, USPHS Training Grant 2A-5067 (C6), and Research Grant RG 8826 from the Division of General Medical Sciences of the National Institutes of Health, USPHS. It is publication number 333 of the Robert W. Lovett Memorial Group for the Study of Diseases Causing Deformities, Harvard Medical School at the Massachusetts General Hospital, Boston, Massachusetts.

² Instructor in Medicine, Harvard Medical School; Assistant in Medicine, Massachusetts General Hospital, Boston, Massachusetts.

³ Resident in Medicine, Massachusetts General Hospital, Boston, Massachusetts.