抄録
1. Bovine globin α obtained from type HbA/HbA was partialy hydrolyzed with trypsin, and the soluble tryptic peptides were resolved on paper sheet two-dimensionally with electrophoresis and then with chromatography.
2. Most of the 16 main spots on the two-dimensional map showed good corres-pondance with each of the tryptic peptides obtained from the human globin α, as to their electrophoretic, and chromatographic, behaviors and to their constituent.
3. Fourteen of the 15 main spots were isolated in homogeneous state and their N-terminal and amino acid composition were compared with those of the corresponding human tryptic peptides.
4. Tryptic core, after being purified by partition chromatography, was further partially hydrolyzed with pepsin and these fragments were also analyzed on the N-terminal and on the composition.
5. From these results, was presumed the partial structure of bovine globin α and these results were discussed.
We were greatly indebted to Miss M. Yoshida, Miss Y. Nagatsuka and Miss F. Kitamura for their technical assistances. This work was partly suported by grant from the Ministry of Education (“Structural Studies on Protein”).
