Abstract
Tryptic peptides and chymotryptic peptides from a polypeptide chain in All component of adult chicken hemoglobin were isolated and purified by using column chromatography and paper chromatography. Furthermore amino acid sequence analyses of these peptides were performed mainly by redigestion with enzyme, the PTC method and the DNP method. From the result of these experiments, the primary structure of this a polypeptide chain was determined. That is, a polypeptide chain in All component from adult chicken hemoglobin consisted of 141 amino acids. In comparison with the primary structure of a polypeptide chain from adult human hemoglobin, amino acid sequence exchanges were found at 35 positions, and with a polypeptide chain from horse hemoglobin, amino acid sequence exchanges were found at 40 positions.
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