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The Complete Amino‐Acid Sequence of Hen Ovalbumin
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The complete amino acid sequence of hen ovalbumin, comprising 385 residues, has been determined. The sequence was deduced from the 17 cyanogen bromide fragments and from peptides derived by digestion with a number of proteolytic enzymes. The molecular weight of the polypeptide chain of ovalbumin is 42699.Ovalbumin has four sites of postsynthetic modification; in addition to the acetylated N terminus, the carbohydrate moiety is located at Asn‐292, and the two phosphorylated serines are at residues 68 and 344. The ‘signal sequence’ of ovalbumin is between residues 234 and 252. The heptapeptide released during the conversion of ovalbumin to plakalbumin by subtilisin digestion corresponds to residues 346–352. The hen ovalbumin polymorphism characterised by an Asn–>Asp replacement results from a mutation at residue 311.The amino acid sequence of ovalbumin deduced from these amino acid sequence studies is in complete agreement with the sequence of mRNA determined by McReynolds et al. [Nature (Lond.) 273, 723–728 (1978)].
Title: The Complete Amino‐Acid Sequence of Hen Ovalbumin
Description:
The complete amino acid sequence of hen ovalbumin, comprising 385 residues, has been determined.
The sequence was deduced from the 17 cyanogen bromide fragments and from peptides derived by digestion with a number of proteolytic enzymes.
The molecular weight of the polypeptide chain of ovalbumin is 42699.
Ovalbumin has four sites of postsynthetic modification; in addition to the acetylated N terminus, the carbohydrate moiety is located at Asn‐292, and the two phosphorylated serines are at residues 68 and 344.
The ‘signal sequence’ of ovalbumin is between residues 234 and 252.
The heptapeptide released during the conversion of ovalbumin to plakalbumin by subtilisin digestion corresponds to residues 346–352.
The hen ovalbumin polymorphism characterised by an Asn–>Asp replacement results from a mutation at residue 311.
The amino acid sequence of ovalbumin deduced from these amino acid sequence studies is in complete agreement with the sequence of mRNA determined by McReynolds et al.
[Nature (Lond.
) 273, 723–728 (1978)].
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