title: The complete amino-acid sequence of the K88 antigen, a fimbrial protein from Escherichia coli.
abstract: 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.
mesh_terms: D000595:Amino Acid Sequence; D000942:Antigens, Bacterial; D000954:Antigens, Surface; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D004926:Escherichia coli / Q000276:immunology*; D029968:Escherichia coli Proteins; D036781:Fimbriae Proteins; D007463:Iodobenzoates; D010446:Peptide Fragments; D014357:Trypsin
chemical_list: D000942:Antigens, Bacterial; D000954:Antigens, Surface; D029968:Escherichia coli Proteins; D007463:Iodobenzoates; C026888:K88 antigen, E coli; D010446:Peptide Fragments; D036781:Fimbriae Proteins; C008154:2-iodosobenzoic acid; D002918:Chymotrypsin; D014357:Trypsin; D003488:Cyanogen Bromide