Open AccessThe Complete Amino‐Acid Sequence of the K88 Antigen, a Fimbrial Protein from Escherichia coli
Author(s) -
KLEMM Per
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb06382.x
Subject(s) - cyanogen bromide , edman degradation , cleavage (geology) , trypsin , protein primary structure , peptide sequence , chemistry , chymotrypsin , biochemistry , amino acid , antigen , peptide , escherichia coli , biology , enzyme , paleontology , genetics , fracture (geology) , gene
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 molecule 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 a molecular anchor.