Secretory Production of Erythropoietin and the Extracellular Domain of the Erythropoietin Receptor by Bacillus brevis : Affinity Purification and Characterization

概要

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Bacillus brevis secretes a large amount of cell wall proteins into the culture medium. For construction of Bacillus brevis expression-secretion vectors of human erythropoietin (EPO) and the extracellular domain of mouse erythropoietin receptor (sEPOR), cDNA for each mature form was inserted into a plasmid containing the promoter region and the signal-peptide encoding region of a cell wall protein. Culture supernatants of transformants were affinity purified using a monoclonal antibody-fixed gel for EPO and an EPO-fixed gel for sEPOR. The atlinity purification efficiently removed unwanted proteins, giving samples with suffciently high purity to analyze amino acid sequences of N-terminal regions and biological activities. Combination of this secretory production and affinity purification may facilitate isolation of a large amount of pure EPO and sEPOR, and is useful for further understanding the molecular mechanism of interaction between EPO and EPOR.
社団法人日本農芸化学会の論文
1997-04-23