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Structural Studies of the Immunoglobulins

III. AMINOETHYLATED TYPE K BENCE-JONES PROTEINS

From the ¹ From the Department of Biochemistry, University of Florida College of Medicine, Gainesville, Florida 32603, and the Division of Biological Sciences, Indiana University, Bloomington, Indiana 47401

Modified techniques suitable for preparation and enzymatic digestion of aminoethylated Bence-Jones proteins are described. Most of the peptides on a tryptic peptide map of aminoethylated Bence-Jones protein Ag have been assigned a number descriptive of their sequence and position in the molecule. Of 24 predicted peptides in a tryptic digest of this Type K protein, 22 have been identified, some tentatively, on a peptide map. Of 13 peptides in the "constant" portion of the molecule, 12 have been identified on the peptide maps of five other aminoethylated Bence-Jones proteins of Type K. The aminoethylcysteinyl peptides of these six proteins have been characterized and, by analogy to known sequences, have been numbered tentatively according to their order in the molecule. Although not all the predicted peptides were identifiable, aminoethylation permits a rapid comparative survey of structural differences among Bence-Jones proteins. One disulfide bridge is in the carboxyl half of the chain, which has an invariant sequence except for a single valine-leucine interchange apparently associated with the Inv genetic factor. The second disulfide bridge in the amino terminal half may vary in position in different Type K proteins and is associated with multiple differences in amino acid sequence.

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