Aitken A
Eur J Biochem. 1977 Aug 15;78(1):273-9. doi: 10.1111/j.1432-1033.1977.tb11738.x.
The amino acid sequence of the soluble c-type cytochrome, cytochrome f, from the cyanobacterium Plectonema boryanum (also called Phormidium luridum or Schizothrix calcicola) has been determined. The proposed sequence consists of one polypeptide chain of 85 residues and has three Asn-Gly linkages. Partly due to the presence of these Asn-Gly bonds, which readily undergo rearrangement, proteolytic digestion on the small amount of protein available was unsatisfactory. The structure was determined partly by a combination of chemical cleavage and automatic sequencing techniques. A new technique for conserving material by cyanogen bromide cleavage of residual polypeptide after automatic degradation is described. The possible evolutionary significance of primary structure comparisons with other cytochromes f is discussed.
已确定来自蓝细菌颤藻（也称为 luridum 席藻或钙质裂须藻）的可溶性 c 型细胞色素细胞色素 f 的氨基酸序列。所提出的序列由一条含 85 个残基的多肽链组成，并有三个天冬酰胺 - 甘氨酸连接。部分由于这些易于重排的天冬酰胺 - 甘氨酸键的存在，对少量可用蛋白质进行的蛋白水解消化并不理想。该结构部分是通过化学裂解和自动测序技术相结合来确定的。描述了一种在自动降解后通过溴化氰裂解残留多肽来保存材料的新技术。还讨论了与其他细胞色素 f 进行一级结构比较可能具有的进化意义。
