@article{oai:nagasaki-u.repo.nii.ac.jp:00021623,
 author = {Maeda, Kenji},
 issue = {3-4},
 journal = {Acta medica Nagasakiensia},
 month = {Mar},
 note = {In order to study the N-terminal structure of rat adult hemoglobin , its heterogeneity was primarily recognized by agar-gel electrophoresis and cellulose-acetate membrane electrophoresis. Then, the main component of rat adult hemoglobin was isolated and purified by column chromatography on CM-cellulose with the elution by the salt concentration gradient of phosphate buffer, and globin was prepared by removing heme from the component. This rat adult globin, examined by urea dissociation electrophoresis using cellulose-acetate membrane, was recognized to contain two kinds of polypeptide chains. On the other hand, this globin was dinitrophenylated to make DNP-globin. This DNP-globin was then hydrolyzed with 6 N HC1 for 1/4, 1, 6, 10 and 20 hr, and from the hydrolysates the DNP-amino acids and DNP-peptides were extracted with ether or ethyl acetate, which were separated, identified and determined quantitatively by silica gel-celite column chromatography and paper chromatography . As the results, it has proved that rat adult globin, just like human adult globin, consists of two polypeptide chains with valylleucyl sequence as the N-terminal structure and two polypeptide chains with valylhistidylleucyl sequence as the Nterminal structure., Acta medica Nagasakiensia. 1966, 10(3-4), p.106-120},
 pages = {106--120},
 title = {Comparative Biochemistry of Hemoglobins},
 volume = {10},
 year = {1966}
}