Hofmann O, Braunitzer G
Max-Planck-Institut für Biochemie, Abt. Proteinchemie, Martinsried bei München.
Biol Chem Hoppe Seyler. 1987 Aug;368(8):949-54. doi: 10.1515/bchm3.1987.368.2.949.
The complete primary structure of the alpha- and beta-chains of the hemoglobin of Spectacled Bear (Tremarctos ornatus) is presented. Following cleavage of the heme-protein link and chain separation by RP-HPLC, their amino-acid sequences were determined by Edman degradation in liquid- and gas-phase sequenators. The hemoglobin of Spectacled Bear displays only five amino-acid exchanges to that of Polar Bear (Ursus maritimus, Ursinae) and Asiatic Black Bear (Ursus tibetanus, Ursinae) whereas 8 and 12 replacements, respectively, to Giant Panda (Ailuropoda melanoleuca) and Lesser Panda (Ailurus fulgens) can be found. This clearly demonstrates that the Spectacled Bear, the most aberrant bear of the Ursidae, is somewhat intermediate between Pandas and Ursinae.
本文展示了眼镜熊（Tremarctos ornatus）血红蛋白α链和β链的完整一级结构。通过反相高效液相色谱法（RP-HPLC）切断血红素与蛋白质的连接并分离链后，利用液相和气相测序仪中的埃德曼降解法测定了它们的氨基酸序列。眼镜熊的血红蛋白与北极熊（Ursus maritimus，熊亚科）和亚洲黑熊（Ursus tibetanus，熊亚科）相比，仅显示出五个氨基酸的替换，而与大熊猫（Ailuropoda melanoleuca）和小熊猫（Ailurus fulgens）相比，分别有8个和12个替换。这清楚地表明，眼镜熊作为熊科中最异常的熊，在熊猫和熊亚科之间处于某种中间位置。
