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Optical Rotatory Dispersion Studies of Rabbit G-Immunoglobulin and Its Papain Fragments

From the ¹ From the Department of Microbiology, Washington University School of Medicine, St. Louis, Missouri, and the Children's Cancer Research Foundation and the Department of Biological Chemistry, Harvard Medical School, Boston, Massachusetts

Certain purified antibodies can be distinguished from nonspecific G-immunoglobulin by optical rotatory dispersion in the ultraviolet region. Thus, inert G-globulin has troughs at 231 mµ ([R'] = -1320) and 224 mµ ([R') = -1240) while anti-2,4-dinitrophenyl (anti-DNP) antibody of high affinity for ligand has its major trough at 224 mµ ([R'] = -1650). The rotatory dispersion of high affinity anti-2,4,6-trinitrophenyl antibody resembles that of low affinity anti-DNP antibody ([R']₂₂₄ = -1300). The characteristic optical rotation of anti-DNP antibody does not appear to be related to variation in allotypy or charge. Furthermore, it is not a consequence of the antibody purification procedure.

The difference in optical rotation between anti-DNP antibody and inert G-globulin is confined to Fab, the active fragment produced by papain digestion. The active fragments of both proteins have troughs at 224 mµ, but that of the antibody is deeper. In contrast, the crystallizable fragments, Fc, are virtually identical, with no trough at 224 but with well defined minima at 233 mµ.

Despite differences in Cotton effects, inert G-globulin and anti-DNP antibody, as well as the corresponding pieces obtained by digestion with papain, are very similar in their over-all conformation as shown by sedimentation and molecular weight studies. Therefore, the variation in optical rotation is probably related to very limited structural differences within the G-immunoglobulins.

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