血红蛋白伍德β97（FG4）处的组氨酸被亮氨酸取代。一种与家族性红细胞增多症相关的新型高氧亲和力血红蛋白。
Hemoglobin Wood beta97(FG4) His replaced by Leu. A new high-oxygen-affinity hemoglobin associated with familial erythrocytosis.
作者信息
Taketa F, Huang Y P, Libnoch J A, Dessel B H
出版信息
Biochim Biophys Acta. 1975 Aug 19;400(2):348-53.
PMID:1164511
Abstract
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).
摘要
本文描述了血红蛋白伍德（β97（FG4）位的组氨酸被亮氨酸取代）的特征，它是一种具有降低的希尔常数的高氧亲和力血红蛋白。氨基酸取代发生在α1β2界面，与血红蛋白马尔默（β97（FG4）位的组氨酸被谷氨酰胺取代）处于相同位置，与血红蛋白切萨皮克（α92（FG4）位的精氨酸被亮氨酸取代）和开普敦J（α92（fg4）位的精氨酸被谷氨酰胺取代）相比处于同源位置。
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