Petruzzelli R, Barra D, Bossa F, Condò S G, Brix O, Nuutinen M, Giardina B
Dipartimento di Biologia, Università di Roma Tor Vergata, Italy.
Biochim Biophys Acta. 1991 Jan 29;1076(2):221-4. doi: 10.1016/0167-4838(91)90270-a.
The primary structures of alpha- and beta-chains of hemoglobin from reindeer (Rangifer tarandus tarandus) were determined. Comparison of the reindeer hemoglobin sequence with those of human and bovine hemoglobins showed 50 and 29 substitutions per alpha beta dimer, respectively. The influence of replacements on the modulation of hemoglobin oxygen affinity by heterothopic ligands and temperature, as well as their importance on the structure-function relationships in hemoglobin are discussed.
确定了驯鹿（Rangifer tarandus tarandus）血红蛋白α链和β链的一级结构。将驯鹿血红蛋白序列与人类和牛血红蛋白序列进行比较，结果显示每个αβ二聚体分别有50个和29个替换位点。讨论了这些替换对异种配体和温度调节血红蛋白氧亲和力的影响，以及它们在血红蛋白结构-功能关系中的重要性。
