Myoglobins of cartilaginous fishes III. Amino acid sequence of myoglobin of the shark Galeorhinus australis.
Myoglobins of cartilaginous fishes III. Amino acid sequence of myoglobin of the shark Galeorhinus australis.
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软骨鱼的肌红蛋白 III．
DOI：
10.1071/bi9810005
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发表时间：
1981
期刊：
影响因子：
--
通讯作者：
E. Thompson
中科院分区：
文献类型：
--
作者：
W. Fisher;D. D. Koureas;E. Thompson
采用凝胶过滤和离子交换色谱法从南方鲨（Galeorhinus australis）红肌中分离纯化肌红蛋白。在用胰蛋白酶消化并通过纸离子电泳和色谱法纯化肽后确定氨基酸序列。纯化的肽的序列通过丹磺酰-埃德曼程序确定，并且肽通过与胶鲨南极鼬的肌红蛋白的序列的同源性比对。这两个肌红蛋白序列显示出明显的相似性（16个差异），但两个序列显示出与波特杰克逊鲨鱼Heterodontus portusjacksoni的肌红蛋白大致相同数量的差异（68个）。三种鲨鱼肌红蛋白序列共有19个氨基酸残基。与其他鱼类肌红蛋白一样，有148个残基，在氨基末端缺失4个残基，在CD区缺失1个残基。氨基末端残基被乙酰化。发现远端E7组氨酸残基被谷氨酰胺取代，如先前仅报道的橡皮糖鲨鱼肌红蛋白序列。
Myoglobin isolated from the red muscle of the school shark Galeorhinus australis was purified by gel filtration and ion-exchange chromatography. The amino acid sequence was determined following digestion with trypsin and purification of the peptides by paper ionophoresis and chromatography. Sequences of purified peptides were determined by the dansyl-Edman procedure and the peptides aligned by homology with the sequence of the myoglobin of the gummy shark Mustelus antarcticus. The two myoglobin sequences showed a marked similarity (16 differences), but both sequences showed approximately the same number of differences (68) from myoglobin of the Port Jackson shark Heterodontus portusjacksoni. There are 19 residues unique to three shark myoglobin sequences. As found with other fish myoglobins there are 148 residues with deletions of four residues at the amino terminal end as well as one residue in the CD region. The amino terminal residue is acetylated. The distal E7 histidine residue was found to be replaced by glutamine, as only previously reported for the myoglobin sequence of gummy shark.