Huber K, Braunitzer G, Schneeganss D, Kösters J, Grimm F
Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.
Biol Chem Hoppe Seyler. 1988 Jun;369(6):513-9. doi: 10.1515/bchm3.1988.369.1.513.
The blood of the Rock-Hopper Penguin contains only one hemoglobin component, corresponding to the Hb A of other birds. The primary structures of the alpha- and beta-chains are presented. The chains were separated by high-performance liquid chromatography and cleaved either enzymatically (alpha) or both enzymatically and chemically (beta). Both the native chains and their peptides were sequenced using liquid and gas phase sequenators. The peptides were aligned using their homology to the sequence of human hemoglobin and other bird hemoglobins. As compared to human hemoglobin, 44 amino-acid replacements are found in the alpha-chains (68% homology) and 47 in the beta-chains (67.8% homology). These exchanges involve seven alpha 1/beta 1 and one alpha 1/beta 2 contact in the alpha-chains, whereas in the beta-chains eight alpha 1/beta 1, one alpha 1/beta 2 and one hem contact are substituted. The influence of these replacements on the structure-function relationships in hemoglobin, as well as their importance for the diving ability of penguins, are discussed.
跳岩企鹅的血液仅含有一种血红蛋白成分，这与其他鸟类的血红蛋白A相对应。文中给出了α链和β链的一级结构。这些链通过高效液相色谱法分离，α链通过酶切（α链），β链则通过酶切和化学切割（β链）。天然链及其肽段均使用液相和气相测序仪进行测序。通过与人类血红蛋白及其他鸟类血红蛋白序列的同源性对肽段进行比对。与人类血红蛋白相比，α链中有44个氨基酸替换（同源性为68%），β链中有47个氨基酸替换（同源性为67.8%）。这些替换在α链中涉及7个α1/β1和1个α1/β2接触点，而在β链中，8个α1/β1、1个α1/β2和1个血红素接触点被取代。文中讨论了这些替换对血红蛋白结构 - 功能关系的影响，以及它们对企鹅潜水能力的重要性。
