Abbasi A, Braunitzer G, Matsuda G, Maita T
Biol Chem Hoppe Seyler. 1986 Apr;367(4):355-61. doi: 10.1515/bchm3.1986.367.1.355.
The complete primary structure of the two major hemoglobin components of sperm whale (Physeter catodon) is presented. The major components A and B account for 55% and 40% respectively whereas the minor component constitutes for 5% of the total hemoglobin. The globin chains were separated on CM-Cellulose in 8M urea buffer. The sequence was determined by automatic Edman degradation of tryptic and hydrolytic peptides in a liquid phase sequencer. Alignment of the sequence with human hemoglobin shows 22 exchanges each for the alpha I and alpha II and 21 exchanges for the beta I and beta II chains. Within the two beta-chains three differences have been located, beta NA2 His/Gln, beta A2 Gly/Ala and beta A8 Leu/Val. The two alpha-chains are characterized by heterogeneities at position alpha A8 Val/Ile or Ala/Ile (ratio of the phenylthiohydantoin derivatives of the amino acids 1:1) and alpha AB1 Asn/Ser (ratio of the phenylthiohydantoin derivatives of the amino acids 6:4). The role of these exchanges in modulating oxygen affinity is discussed.
本文给出了抹香鲸（Physeter catodon）两种主要血红蛋白成分的完整一级结构。主要成分A和B分别占55%和40%，而次要成分占总血红蛋白的5%。球蛋白链在8M尿素缓冲液中于CM-纤维素上分离。序列通过在液相测序仪中对胰蛋白酶和水解肽进行自动埃德曼降解来确定。该序列与人血红蛋白的比对显示，αI和αII链各有22个置换，βI和βII链有21个置换。在两条β链中定位到了三个差异，βNA2 His/Gln、βA2 Gly/Ala和βA8 Leu/Val。两条α链的特征在于αA8位置的异质性，Val/Ile或Ala/Ile（氨基酸苯硫代乙内酰脲衍生物的比例为1:1）以及αAB1 Asn/Ser（氨基酸苯硫代乙内酰脲衍生物的比例为6:4）。讨论了这些置换在调节氧亲和力中的作用。
