Lehman L D, Jones B N, Dwulet F E, Bogardt R A, Gurd F R
Biochim Biophys Acta. 1980 Oct 21;625(2):221-9. doi: 10.1016/0005-2795(80)90285-8.
The complete primary structure of the major component myoglobin from the goose-beaked whale, Ziphius cavirostris, was determined by specific cleavage of the protein to obtain large peptides which are readily degraded by the automatic sequencer. Over 80% of the amino acid sequence was established from the three peptides resulting from the cleavage of the apomyoglobin at its two methionine residues with cyanogen bromide along with the four peptides resulting from the cleavage with trypsin of the citraconylated apomyoglobin at its three arginine residues. Further digestion of the central cyanogen bromide peptide with S. aureus strain V8 protease and the 1,2-cyclohexanedione-treated central cyanogen bromide peptide with trypsin enabled the determination of the remainder of the covalent structure. This myoglobin differs from the cetacean myoglobins determined to date at 12 to 17 positions. These large sequence differences reflect the distant taxonomic relationships between the goose-beaked whale and the other species of Cetacea the myoglobin sequences of which have previously been determined.
通过对鹅喙鲸（Ziphius cavirostris）主要成分肌红蛋白进行特异性切割，获得易于被自动测序仪降解的大肽段，从而确定了其完整的一级结构。通过用溴化氰在两个甲硫氨酸残基处切割脱辅基肌红蛋白产生的三个肽段，以及用胰蛋白酶在三个精氨酸残基处切割柠康酰化脱辅基肌红蛋白产生的四个肽段，确定了超过80%的氨基酸序列。用金黄色葡萄球菌V8蛋白酶对中央溴化氰肽进行进一步消化，并用胰蛋白酶对经1,2 - 环己二酮处理的中央溴化氰肽进行消化，从而确定了共价结构的其余部分。这种肌红蛋白与迄今已确定的鲸类肌红蛋白在12至17个位置上存在差异。这些较大的序列差异反映了鹅喙鲸与其他已确定肌红蛋白序列的鲸目物种之间遥远的分类关系。
