Purification and characterization of a low and a high molecular weight form of epidermal growth factor from rat urine.
Two forms of epidermal growth factor (EGF) have been purified to homogeneity from rat urine by immunoaffinity chromatography and gel filtration. For one of the purified peptides the molecular mass has been determined to be 5891 by mass spectrometry. This peptide consists of 51 amino acid residues. The sequence of the first 48 amino acid residues is identical to the previously published sequence for submandibular rat EGF. The C-terminal three residues (49-51) are Trp-Trp-Lys. The other purified peptide has a molecular mass of 45 kDa as determined by SDS-polyacrylamide gel electrophoresis. The N-terminal sequence is Asn-Tyr-Lys-Asp-(Cys)-Gly-Pro-Gly-Gly-(Cys)-Gly-Ser-His-Ala. Both the high and the low molecular mass form of urinary rat EGF are able to bind to the human placenta receptor for EGF.
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Department of Clinical Chemistry, Central Hospital, Hillerød, Denmark.
Jørgensen
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Thim
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Roepstorff
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D000595:Amino Acid Sequence; D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004815:Epidermal Growth Factor / Q000302:isolation & purification / Q000652:urine*; D066246:ErbB Receptors / Q000378:metabolism; D006801:Humans; D007118:Immunoassay; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D051381:Rats; D011919:Rats, Inbred Strains; D014357:Trypsin
D004815:Epidermal Growth Factor; D066246:ErbB Receptors; D014357:Trypsin