The N-terminal structure of adult hemoglobin from Japanese monkey (Macaca fuscata fuscata) and the N-terminal amino acids of all the tryptic peptides from its alpha and beta polypeptide chains.

The N-terminal structure of adult Japanese monkey (macaca fuscata fuscata) hemoglobin and the N-terminal amino acid analyses of the tryptic peptides from this hemoglobin were performed. Hemoglobin, after removal of heme, was dinitrophenylated. The DNP-globin was hydrolyzed with HCl, and from the hydrolysate DNP-derivatives were extracted with ether or ethyl acetate. They were isolated and identified by silica gel-Celite column chromatography, and quantitative analyses were performed by spectrophotometry. Consequently, it was known that one mole of hemoglobin of the Japanese monkey consisted of two polypeptide • @ chains • @whose • @N-terminal • @ structure • @ was • @ Val-Leu(ƒ¿. • @chains)and two • @ polypeptide • @ chains • @whose • @N-terminal • @ structure • @ was • @Val-His-Leu(ƒÀ chains). • @ On • @ the • @ other • @hand, • @ globin • @was • @separated • @ into • @the • @subunits, • @ ƒ¿ and,ƒÀ • @ polypeptide • @ chains • @by • @ countercurrent • @ distribution. • @Each • @ polypeptide chain was hydrolyzed with trypsin. The hydrolyzed peptides were isolated and purified by column chromatography and paper chromatography. The N-terminal amino acids of the peptides thus isolated and purified were discussed by comparing with human hemoglobin. It was known that the N-terminal • @ sturcture • @ of,ƒÀT2 • @peptide • @ consisted • @ of • @ serine • @ in • @ the • @case • @of • @ human hemoglobin, but asparagine in the case of Japanese monkey hemoglobin and that other 21 peptides has same N-terminal amino acids as those from human hemoglobin do, respectively.