Abstract
Globin prepared from hemoglobin of the brown lemur (Lemur fulvus fulvus) was separated into α and β chains by chromatography on a CM 52 column. The S-aminoethylated α and β chains were each digested with trypsin and resulting peptides were isolated. The amino acid sequences of the tryptic peptides were established. The ordering of these peptides in the α and β chains was deduced from the homology of their amino acid sequences with that of human adult hemoglobin. The primary structure of brown lemur hemoglobin thus obtained differs from that of human hemoglobin in 15 amino acids in the α chain and 26 in the β chain.
