Abstract
The amino acid sequence of the a-chain of haemoglobin from M. giganteus has been determined. The soluble peptides formed by tryptic digestion were isolated by gel filtration, ion-exchange chromatography, paper ionophoresis, and chromatography. The amino acid sequences were determined by the "dansyl"Edman procedure. Incomplete hydrolysis of one bond resulted in a large insolublecore peptide containing 40 amino acid residues. The sequence of this peptide was deduced from the sequences of smaller peptides resulting from further digestion with thermolysin and papain. Maleylation of the a-globin before tryptic digestion gave three large fragments which assisted in assigning tryptic peptides to specific areas of the molecule. A special procedure involving maleylation of a chymotryptic digest of globin was used to isolate peptides containing arginine which provided overlap sequences of tryptic peptides
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