Hemoglobin Wood beta97(FG4) His replaced by Leu. A new high-oxygen-affinity hemoglobin associated with familial erythrocytosis.

Autor: Taketa F, Huang YP, Libnoch JA, Dessel BH
Jazyk: angličtina
Zdroj: Biochimica et biophysica acta [Biochim Biophys Acta] 1975 Aug 19; Vol. 400 (2), pp. 348-53.
Abstrakt: The characterization of hemoglobin Wood (beta97(FG4) His replaced by Leu), a high oxygen affinity hemoglobin with reduced Hill constant is described. The amino acid substitution occurs at the alpha1beta2 interface, in the same position as in hemoglobin Malmö (beta97(FG4) His replaced by Gln) and in an homologous position when compared with hemoglobins Chesapeake (alpha92(FG4) Arg replaced by Leu) and J. Capetown (alpha92(fg4) arg replaced by Gln).
Databáze: MEDLINE