The complete amino acid sequence of the major component myoglobin of Amazon river dolphin (Inia geoffrensis).
The complete amino acid sequence of the major component myoglobin of Amazon river dolphin (Inia geoffrensis).
复制标题
亚马逊河豚 (Inia geoffrensis) 主要成分肌红蛋白的完整氨基酸序列。
DOI:
10.1021/bi00695a018
复制
发表时间:
1975
期刊:
影响因子:
2.9
通讯作者:
F. Gurd
中科院分区:
文献类型:
--
作者:
F. Dwulet;R. Bogardt;B. Jones;L. Lehman;F. Gurd
The complete amino acid sequence of the major component myoglobin from Amazon River dolphin, Inia geoffrensis, was determined by specific cleavage of the protein to obtain large peptides which are readily degraded by the automatic sequencer. Three easily separable peptides were obtained by cleaving the protein with cyanogen bromide at the methionine residues and four peptides were obtained by cleaving the methyl-acetimidated protein with trypsin at the arginine residues. From these peptides over 85% of the sequence was completed. The remainder of the sequence was obtained by fragmentation of the large cyanogen bromide peptide with trypsin. This protein differs from that of the common porpoise, Phocoena phocoena, at seven positions, from that of the common dolphin, Delphinus delphis, at 11 positions, and from that of the sperm whale, Physeter catodon, at 15 positions. By comparison of this sequence with the three-dimensional structure of sperm whale myoglobin it appears that those residues close to the heme group are most conserved followed by those in nonhelical regions and lastly by those in the helical segments. All of the substitutions observed in this sequence fit easily into the three-dimensional structure of the sperm whale myoglobin.