Kunihiro Koshikawa

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One of the components of hemoglobin from the larval hemolyph of Tokunagayusurika akamusi possesses naturally occurring substitution at the E7 helical position (Leu E7) [M. Fukuda, T. Takagi, K. Shikama, Biochim. Biophys. Acta 1157 (1993) 185-191]. Its oxygen affinity is almost comparable to those of mammalian myoglobins and it exhibits Bohr effect. Both(More)
The functional properties of the Arg residue at the E10 helical position in myoglobin and hemoglobin lacking the highly conserved His residue at the E7 position have received considerable interest as to the structure-function relationship of the oxygen-binding hemoproteins, because Arg E10 in such proteins has been shown to play similar roles to those His(More)
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