Klemm P
Eur J Biochem. 1981 Jul;117(3):617-27. doi: 10.1111/j.1432-1033.1981.tb06382.x.
The complete primary structure of the fimbrial protein of the K88 antigen has been elucidated. This protein, which makes up the building block for the macromolecular structure that comprises a fimbria, consists of 264 amino acid residues in a single polypeptide chain. The K88 antigen was fragmented by chemical cleavage with cyanogen bromide, and by subsequent enzymatic sub-cleavage of resulting fragments with trypsin and chymotrypsin, and was additionally cleaved with o-iodosobenzoic acid. Peptides were sequenced by manual Edman degradation. The carboxy-terminal part of the molecular is remarkable in being almost devoid of charged amino acid residues and is highly hydrophobic. Furthermore, this part of the structure could have a specific function as molecular anchor.
K88抗原菌毛蛋白的完整一级结构已被阐明。这种构成菌毛大分子结构基本单元的蛋白质，由一条单多肽链中的264个氨基酸残基组成。K88抗原经溴化氰化学裂解，以及用胰蛋白酶和糜蛋白酶对所得片段进行后续酶促亚裂解，并额外用邻碘苯甲酸裂解。肽段通过手动埃德曼降解法测序。该分子的羧基末端部分显著特点是几乎没有带电荷的氨基酸残基，且高度疏水。此外，该结构部分可能具有作为分子锚的特定功能。
