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Amino Acid Sequence of Human Chains

III. TRYPTIC PEPTIDES, CHYMOTRYPTIC PEPTIDES, AND SEQUENCE OF PROTEIN Bo

From the ¹ From the Department of Zoology, Indiana University, Bloomington, Indiana 47401

The primary structure of the variable region of the human Bence-Jones Protein Bo has been determined by sequence analysis of the tryptic peptides from the aminoethylated protein and the chymotryptic peptides from the carboxymethylated protein. The primary structure of the constant region has been adduced by partial sequence analysis of the tryptic peptides, from the composition of the chymotryptic peptides, and by homology to other human chains. Twenty-three tryptic peptides covering the entire protein and 32 chymotryptic peptides covering all but 8 of the total of 216 residues were isolated. The position of 148 residues was determined directly by Edman degradation and enzymatic digestion or by the overlapping of peptides. The remainder were placed by homology. Compared to the reference chain Sh, Protein Bo has additional residues at four new positions (the NH₂ terminus and positions 27a, 27b, and 27c) and lacks a residue at position 96 (des-96). Residues 109 through 213 appear identical with the sequence reported for Protein Sh and four other chains that have been sequenced, but from 30 to 50 residues differ in the first or variable half of chains. The calculated molecular weight of the monomeric form of Protein Bo is 22,982.

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