Complete amino acid sequence of myoglobin from the pilot whale, Globicephala melaena.
Complete amino acid sequence of myoglobin from the pilot whale, Globicephala melaena.
复制标题
领航鲸 Globicephala melaena 肌红蛋白的完整氨基酸序列。
DOI：
10.1021/bi00603a027
复制
发表时间：
1978
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：
B. Jones;F. Dwulet;L. Lehman;M. Garner;R. Bogardt;W. Garner;F. Gurd
从领航员鲸（gloicephala melaena）中提取的主要成分肌红蛋白的完整氨基酸序列，通过对该蛋白进行特异性切割以获得易于被自动测序仪降解的大肽。用溴化氰选择性地在2个蛋氨酸基残基上进行酶切，用胰蛋白酶选择性地在3个精氨酸基残基上进行酶切。通过对其中4个多肽和载脂蛋白的序列分析，获得了该蛋白90%以上的共价结构。其余的一级结构是通过对从中心溴化氰片段分离的三个色氨酸肽的序列分析确定的，这些片段是在用1,2-环己二酮修饰其单一精氨酸残基后分离出来的。这种肌红蛋白与黑海海豚的肌红蛋白有四个位置不同，与虎鲸、太平洋普通海豚和大西洋宽吻海豚的肌红蛋白有两个位置不同。上述差异反映了这五种鲸目动物在分类上的密切关系。该序列测定由德州仪器980A微型计算机系统辅助，该系统对所有样品进行氨基酸分析的峰整合。
The complete amino acid sequence of the major component myoglobin from the pilot whale, Globicephala melaena, was determined by specific cleavage of the protein to obtain large peptides which are readily degraded by the automatic sequencer. The apomyoglobin was selectively cleaved at the two methionyl residues with cyanogen bromide and the acetimidated apomyoglobin was cleaved at the three arginyl residues by trypsin. From the sequence analysis of four of these peptides and the apoprotein, over 90% of the covalent structure of the protein was obtained. The remainder of the primary structure was determined by sequence analysis of three of the tryptic peptides isolated from the central cyanogen bromide fragment after modification of its single arginyl residue with 1,2-cyclohexanedione. This myoglobin differs from that of the Black Sea dolphin at four positions and from the myoglobin of the killer whale, Pacific common dolphin, and Atlantic bottlenosed dolphin at two positions. The above differences reflect the close taxonomic relationship of these five species of Cetacea. This sequence determination was aided by the use of a Texas Instruments 980A minicomputer system which performed peak integrations for all samples subjected to amino acid analysis.