Abstract
The reduced and carboxymethylated H-chain of protein Nie [from human myeloma] was digested with trypsin. Forty tryptic peptides were isolated from the digest by ion exchange chromatography, accounting for the entire amino acid composition of the polypeptide chain. Sequence studies performed with these fragments revealed the position of 444 of 448 residues. In addition 8 overlapping cleavage products were purified which contributed to the ordering of tryptic peptides in the chain.