Purification and characterization of high molecular weight human epidermal growth factor from human urine

Biochem Biophys Res Commun. 1987 May 29;145(1):126-33. doi: 10.1016/0006-291x(87)91296-4.

Abstract

High molecular weight human epidermal growth factor (HMW-hEGF) was purified to homogeneity from human urine. The purification was achieved exclusively by the use of immunoaffinity chromatography and reverse phase high performance liquid chromatography (HPLC). The purified HMW-hEGF is composed of a single polypeptide chain with an apparent molecular weight of 30,000 and has pI of 4.0. Its N-terminal sequence was determined as Val-Ser-Asp-Gln-Asp-Asp-( )-Ala-Pro-Val-Gly-( )-Ser-Met-Tyr-Ala-Arg-( )-Ile- Ser-. The trypsin treatment of this protein gave hEGF like fragments. These results suggest that the obtained HMW-hEGF may play an important role in biosynthetic precursor of hEGF.

MeSH terms

  • Adult
  • Chromatography, Affinity
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Epidermal Growth Factor / genetics
  • Epidermal Growth Factor / isolation & purification
  • Epidermal Growth Factor / urine*
  • Escherichia coli / genetics
  • Genes
  • Humans
  • Male
  • Molecular Weight
  • Recombinant Proteins / isolation & purification

Substances

  • Recombinant Proteins
  • Epidermal Growth Factor