Purification and characterization of high molecular weight human epidermal growth factor from human urine.
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.
Tsukumo
K
K
Nakamura
H
H
Sakamoto
S
S
D000328:Adult; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004815:Epidermal Growth Factor / Q000235:genetics / Q000302:isolation & purification / Q000652:urine*; D004926:Escherichia coli / Q000235:genetics; D005796:Genes; D006801:Humans; D008297:Male; D008970:Molecular Weight; D011994:Recombinant Proteins / Q000302:isolation & purification
D011994:Recombinant Proteins; D004815:Epidermal Growth Factor