Identification of betacellulin as a major peptide growth factor in milk: purification, characterization and molecular cloning of bovine betacellulin
Autor: | A J, Dunbar, I K, Priebe, D A, Belford, C, Goddard |
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Rok vydání: | 1999 |
Předmět: |
Base Sequence
Epidermal Growth Factor Molecular Sequence Data 3T3 Cells Milk Proteins Binding Competitive Cell Line ErbB Receptors Mice Animals Intercellular Signaling Peptides and Proteins Cattle Amino Acid Sequence RNA Messenger Betacellulin Cloning Molecular Growth Substances Digestive System Research Article |
Zdroj: | The Biochemical journal. |
ISSN: | 0264-6021 |
Popis: | Betacellulin (BTC), a member of the epidermal growth factor (EGF) family of peptide growth factors, was purified from a growth-factor-enriched whey fraction of bovine milk by a combination of ion-exchange chromatography, gel-filtration chromatography, affinity chromatography and reverse-phase HPLC. Bovine BTC (bBTC) had an apparent molecular mass of 21-22 kDa on SDS/PAGE and exists in a glycosylated form. The cDNA encoding bBTC was obtained by a combination of 5' and 3' rapid amplification of cDNA ends ('RACE'). The primary translation product consists of 178 amino acid residues containing a putative signal sequence, a transmembrane domain, the mature BTC domain and a cytoplasmic domain containing a highly hydrophilic Arg-Lys-rich region similar to that of mouse BTC and human BTC. The amino acid sequence of the bBTC precursor was 88% identical with human BTC and 79% identical with mouse BTC. The bBTC gene was found to be expressed in a wide range of tissues, including the mammary gland. The identification of BTC in milk raises the possibility that it has a major role in the growth and development of the neonatal gastrointestinal tract. |
Databáze: | OpenAIRE |
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