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A New Serum Factor in Normal Rabbits

VIII. Isolation and Characterization of a Buried Antigenic IgG Determinant¹

From the Department of Microbiology, The University of Texas at Austin, Austin, Texas 78712

Abstract

A hexapeptide was specifically cleaved from the C-terminus of the Fd of rabbit (Fab')₂ fragments. The amino acid composition and sequence of the peptide was identical to that reported for the hinge peptide. These studies further showed that the hinge peptide could be recovered as a disulfide bonded dimer from d11 but not from d12 (Fab')₂ fragments by digestion with CNBr.

The results of this investigation also demonstrated that the isolated peptides were reactive with a specific natural antiglobulin factor in rabbit sera, namely, homoreactant. As such, the peptide represents one of the smallest naturally occurring antigenic determinants isolated from a protein.

The chemical and serological properties of the isolated hinge peptide were confirmed by comparison with a synthetic peptide of determined amino acid sequence.

Footnotes

¹ This study was supported by a United States Public Health Service Grant AI-07184 and Robert A. Welch Foundation Grant F-209. This paper was presented in part at the annual meeting of the Federation of American Society of Experimental Biology, Atlantic City, May 1970.

² Recipient of a United States Public Health Predoctoral Fellowship. Present address: Department of Experimental Biology, Baylor College of Medicine, Houston, Texas.

³ Recipient of a United States Public Health Career Development Award.

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