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An Unusual Papain Fragment Containing the V_H Region of an IgG3 Myeloma Protein¹

From the New York University School of Medicine, Department of Medicine, New York, New York 10016

Abstract

A new enzymatic fragment resulting from papain digestion of an IgG3k myeloma cryoglobulin (protein KUP) is described. This fragment, which can be easily separated from the remainder of the Fab fragment by filtration on Sephadex G-100 in 1 N acetic acid, does not react with a panel of antisera in double diffusion experiments, has a blocked amino-terminal residue and was shown to correspond to most of the heavy chain variable region. It has been tentatively designated Fd_v.

Fd_v is readily soluble in acidic buffers, has a molecular weight of 11,900, a sedimentation coefficient of 1.7S in 1 N acetic acid and contains about 100 residues.

Attempts to isolate, under the same conditions, an analogous fragment from two additional IgG3 and one IgG1 myeloma proteins and from pooled human Cohn FII were unsuccessful. Whether production of Fd_v is a unique property of protein KUP or is related to an unusual V_H subgroup or other factors, remains, so far, undetermined.

Footnotes

¹ This work was supported by United States Public Health Service Grants AMO 1431 and 2594, the New York Chapter of the Arthritis Foundation, Inc. and N.A.T.O.

² On leave of absence from the University of Bari Medical School, Clinica Medica II, Bari, Italy.

³ Career Scientist of the Health Research Council of the City of New York.

⁴ Senior Investigator of the Arthritis Foundation, Inc.