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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 α andβ Polypeptide Chains


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Title: 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 α andβ Polypeptide Chains
Authors: Tanaka, Yoshiro
Authors (alternative): 田中, 義郎
Issue Date: 25-Mar-1969
Citation: Acta medica Nagasakiensia. 1969, 13(3-4), p.211-227
Abstract: 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 DNPglobin 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(α. chains)and two polypeptide chains whose N-terminal structure was Val-His-Leu(β chains). On the other hand, globin was separated into the subunits, α and,β 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 Nterminal sturcture of,βT2 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.
URI: http://hdl.handle.net/10069/15549
ISSN: 00016055
Type: Departmental Bulletin Paper
Text Version: publisher
Appears in Collections:Volume 13, No. 3-4

Citable URI : http://hdl.handle.net/10069/15549

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