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Identification of Heavy Chain Tyrosine 33 in the Binding Site of Myeloma Protein McPC 603 by Paired Label Iodination¹

From the Department of Immunology Research, Roswell Park Memorial Institute,² 666 Elm Street, Buffalo, New York 14263

Abstract

The phosphorylcholine binding mouse myeloma protein McPC 603 has been shown to have tyrosyl residues in its binding sites by the fact that iodination of the protein causes extensive loss of binding activity which can be substantially retained when the protein is iodinated with sites occupied by ligand. Paired label iodination of McPC 603 protein allowed identification of the tyrosine involved and showed the tyrosine to be in the heavy chain. Gel filtration of heavy chain peptides enabled the tyrosyl-containing peptide of interest to be identified as the N-terminal 33 residue peptide in which the only tyrosine is Tyr 33. Thus H chain Tyr 33 was shown to be a contact amino acid residue in the site of McPC 603 protein. These results provide chemical evidence confirming previously reported x-ray crystallographic identification of H chain Tyr 33 in the site of McPC 603 protein.

Footnotes

¹ This work was supported in part by Public Health Service Research Grant CA-11656 and AI-12100.

² A unit of the New York State Department of Health.