Boehringer Ingelheim (Germany)
ORCID: 0000-0002-7508-7281Publishes on Glycosylation and Glycoproteins Research, HER2/EGFR in Cancer Research, Monoclonal and Polyclonal Antibodies Research. 39 papers and 3.2k citations.
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A new procedure has been devised for the preparation of pure epidermal growth factor in high yield. The method involves a two-step column fractionation of crude extracts of the submaxillary gland obtained from adult male mice. Biologically active epidermal growth factor lacking the COOH-terminal Leu-Arg residues was also isolated.
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.
The three disulfide bridges in epidermal growth factor have been identified by the isolation of three unique cystinyl peptides obtained by thermolytic digestion. The cysteic acid-containing peptide pairs derived from each of the cystinyl peptides were isolated. Their amino acid compositions were in agreement with those predicted from the known amino acid sequence of epidermal growth factor. The cysteinyl residues in positions 6 and 20, 14 and 31, and 33 and 42 were linked as disulfides in this 53 amino acid residue polypeptide.