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The Primary Structure of Epidermal Growth Factor

1972; Elsevier BV; Volume: 247; Issue: 23 Linguagem: Inglês

10.1016/s0021-9258(19)44569-9

1083-351X

C. Richard Savage, Tadashi Inagami, Stanley Cohen,

Cancer-related gene regulation

The complete amino acid sequence of epidermal growth factor (EGF) has been established through the use of automated Edman degradation and standard enzymatic and chemical techniques. The location of the half-cystinyl residues was facilitated by the use of the S-[14C]aminoethyl derivative of EGF. The sequence is: [see PDF for sequence]. The calculated molecular weight of the 53-residue polypeptide is 6045, a value that is in agreement with the molecular weight of 6400 established by physical measurements. The peptide is acidic and the 6 half-cystines exist in disulfide linkage. Four arginine residues are located in the COOH-terminal portion of the molecule. The six COOH-terminal amino acids are not necessary for biological activity and EGF1–47 has activity identical with that of the 53-residue native molecule.