caa a22 4500 397555318 CHVBK 20180308164800.0 cr unu---uuuuu 161202e199602 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021248 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021248 Identification of Five Embryonic Hemoglobins of Rat and Ontogeny of Their Constituent Globins during Fetal Development [Elektronische Daten] [Shin-ichiro Iwahara, Yasuko Abe, Taro Okazaki] Hemoglobins of rats switch from an embryonic to an adult type during fetal development. However, very little is known about the structures and molecular species of hemoglobins occurring in the fetal life of rats. In the present study we isolated five embryonic hemoglobins, designated El, E2, E3, E4, and E5, from the blood of rat fetuses on day 14 of gestation by ion exchange chromatography. Reverse-phase high performance liquid chromatography revealed that these hemoglobins each consist of two kinds of globins: E1(11α:ε1), E2(1α:ε1), E3(ζ:ε1), E4(1α:ε3), and E5(ζ:ε3), respectively. The complete ami no acid sequences of the ζ, ε1, and ε3 globins were determined. The ζ globin showed characteristic features common in α-type embryonic globins of known species in that the N-terminus is blocked and the amino acid at position 38 is Gin. ε1 and ε3 are β-type embryonic globins, sharing 73.7% amino acid homology. Interestingly, they are more similar to the corresponding mouse β-type embryonic globins, y and z, respectively, than to each other, implying that these globins have evolved orthologously from common ancestral proteins. It was also shown that the ζ, ε1, and ε3 globins are almost completely replaced by the adult type α and β globins in the blood of rat fetuses by day 18 of gestation. © by the Journal of Biochemistry Regular Papers nationallicence embryonic hemoglobin nationallicence hemoglobin switching nationallicence primary structure nationallicence rat nationallicence zeta and epsilon globins nationallicence Iwahara Shin-ichiro Department of Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyo-ku, Tokyo 113 aut Abe Yasuko Department of Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyo-ku, Tokyo 113 aut Okazaki Taro Department of Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyo-ku, Tokyo 113 aut The Journal of Biochemistry Oxford University Press 119/2(1996-02), 360-366 0021-924X 119:2<360 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021248 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021248 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Iwahara Shin-ichiro Department of Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Abe Yasuko Department of Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Okazaki Taro Department of Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/2(1996-02), 360-366 0021-924X 119:2<360 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford