Fisher W K, Koureas D D, Thompson E O
Aust J Biol Sci. 1980 May;33(2):153-67. doi: 10.1071/bi9800153.
Myoglobin isolated from red muscle of the gummy shark M. antarcticus was purified by gel filtration and ion-exchange chromatography on carboxymethyl cellulose in 8 M urea-thiol buffer. Amino acid analysis and sequence determination showed 148 amino acid residues. The amino terminal residue is acetylated as shown by nuclear magnetic resonance and mass spectrographic analysis of an N-terminal peptide. There is a deletion of four residues at the amino terminal end as well as one residue in the CD interhelical area relative to other myoglobins. These overall differences were also found previously in myoglobin of Heterodontus portusjacksoni. The complete amino acid sequence has been determined following digestion with trypsin, chymotrypsin, thermolysin, staphylococcal protease and cyanogen bromide. Sequences of purified peptides were determined by the dansyl-Edman procedure. The amino acid sequence showed approximately 88 differences from mammalian, monotreme, bird and tuna myoglobins, slightly more than previously reported for H. portusjacksoni usually considered a more primitive animal. There were 24 residues common to both shark myoglobins that were different from those present in other myoglobins. The sequence has been compared to the myoglobin of yellowfin tuna and other myoglobins.
从南极星鲨红色肌肉中分离出的肌红蛋白，通过在8M尿素-硫醇缓冲液中用羧甲基纤维素进行凝胶过滤和离子交换色谱法进行纯化。氨基酸分析和序列测定显示有148个氨基酸残基。如通过对N端肽段的核磁共振和质谱分析所示，氨基末端残基被乙酰化。相对于其他肌红蛋白，在氨基末端有四个残基缺失，并且在CD螺旋间区域有一个残基缺失。这些总体差异先前在杰克逊港异齿鲛的肌红蛋白中也被发现。在用胰蛋白酶、胰凝乳蛋白酶、嗜热菌蛋白酶、葡萄球菌蛋白酶和溴化氰消化后，已确定了完整的氨基酸序列。通过丹磺酰-埃德曼法测定纯化肽段的序列。氨基酸序列显示与哺乳动物、单孔目动物、鸟类和金枪鱼的肌红蛋白大约有88个差异，略多于先前报道的通常被认为是更原始动物的杰克逊港异齿鲛。两种鲨鱼肌红蛋白共有24个与其他肌红蛋白中不同的残基。该序列已与黄鳍金枪鱼的肌红蛋白和其他肌红蛋白进行了比较。
