Abstract

The a polypeptide chain of adult hemoglobin of the rhesus monkey was digested with trypsin. All the tryptic peptides thus obtained were isolated and purified by column and paper chromatography and amino acid sequence analyses of these peptides were performed mainly by partial hydrolyses with enzymes, the DNP method, and the PTC method. The comparison of the results with the known sequences of the corresponding peptides from the a polypeptide chain of human hemoglobin showed that there were four differences in amino acid sequences of these peptides between rhesus monkey and humans.

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