The primary structure of human EGF produced by genetic engineering, studied by high-performance tandem mass spectrometry.

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Citation

Furuya M, Akashi S, Hirayama K

The primary structure of human EGF produced by genetic engineering, studied by high-performance tandem mass spectrometry.

Biochem Biophys Res Commun. 1989 Sep 15;163(2):1100-6.

PubMed ID
2789514 [ View in PubMed
]
Abstract

The primary structure of human epidermal growth factor (hEGF), which was produced by Escherichia coli using recombinant DNA technique, has been studied by tandem mass spectrometry. The molecular weight of hEGF (about 6200 amu) was determined by fast atom bombardment mass spectrometry. Then reduced and carboxymethylated hEGF was digested by chymotrypsin into seven peptides which could cover the whole sequence of hEGF. The amino acid sequences of five of these seven peptides could be confirmed by tandem mass spectrometry with or without isolation by high-performance liquid chromatography (HPLC). After isolation by HPLC, the other two peptides were digested with trypsin or thermolysin into small peptides, and sequenced by tandem mass spectrometry.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Pro-epidermal growth factorP01133Details