Chin C C, Niehaus W G, Wold F
Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston 77225.
J Protein Chem. 1989 Apr;8(2):165-71. doi: 10.1007/BF01024941.
Cytochrome c from Aspergillus niger consists of two forms, a major one (80%) with 111 amino acid residues and a minor one (20%) with 108 residues, missing the three N-terminal residues of the major one. The primary sequence of A. niger cytochrome c was determined by standard spinning-cup Edman degradation of purified peptides and of pairs of peptides, from which the desired sequence was readily deduced by subtraction of common sequencies. Except for the extension and some variability at the N-terminal sequence, the A. niger protein conforms well with other cytochrome c structures.
黑曲霉细胞色素c由两种形式组成，一种主要形式（80%）含有111个氨基酸残基，另一种次要形式（20%）含有108个残基，缺少主要形式的三个N端残基。黑曲霉细胞色素c的一级序列通过对纯化肽段和成对肽段进行标准的旋转杯式埃德曼降解来确定，通过减去共同序列可以很容易地推导出所需序列。除了N端序列的延伸和一些变异性外，黑曲霉蛋白质与其他细胞色素c结构非常吻合。
