Biomaterial Database

A correction and extension of the acetylated amino terminal sequence of ovalbumin. 1978

E O Thompson, and W K Fisher

The acetylpeptides derived from S-carboxymethylovalbumin by cyanogen bromide and chymotrypsin have been isolated and shown by enzyme digestion and the dansyl-Edman method to fit the sequence acetyl-Gly-Ser-Ile-Gly-Ala-Ala-Ser-Met-Glu-Phe. This corrects the order of the third and fourth residues in the five-residue sequence given by Narita and Ishii [J. Biochem. (Tokyo), 1962, 52, 367--73]. The overlap of the C-terminal sequence of this extended sequence with the six-residue N-terminal sequence surrounding a half-cystine residue in ovalbumin gives the N-terminal sequence for ovalbumin as acetyl-Gly-Ser-Ile-Gly-Ala-Ala-Ser-Met-Glu-Phe-Cys-Phe-Asp-Val-Phe-Lys with residue 11 a cysteine residue.

UI	MeSH Term	Description	Entries
D010047	Ovalbumin	An albumin obtained from the white of eggs. It is a member of the serpin superfamily.	Serpin B14
D010455	Peptides	Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS.	Peptide,Polypeptide,Polypeptides
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein