Fusion to an endoglucanase allows alkaline phosphatase to bind to cellulose

Endoglucanase CenA of Cellulomonas fimi comprises an N-terminal cellulose-binding domain and a C-terminal catalytic domain joined together by a sequence of 23 proline and threonine residues (the Pro-Thr box). The domains function independently when separated by proteolysis. Tn phoA has been used to...

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Veröffentlicht in:FEBS letters 1989-02, Vol.244 (1), p.127-131
Hauptverfasser: Greenwood, Jeffrey M., Gilkes, Neil R., Kilburn, Douglas G., Miller, Robert C., Warren, R.Antony J.
Format: Artikel
Sprache:eng
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Zusammenfassung:Endoglucanase CenA of Cellulomonas fimi comprises an N-terminal cellulose-binding domain and a C-terminal catalytic domain joined together by a sequence of 23 proline and threonine residues (the Pro-Thr box). The domains function independently when separated by proteolysis. Tn phoA has been used to generate cenA′-′ phoA fusions. CenA′-′PhoA fusion polypeptides which contain the entire cellulose-binding domain of CenA bind to cellulose, allowing their purification from periplasmic extracts in a single, facile step. This result has implications for purification or immobilisation of chimeric proteins on a cheap cellulose matrix.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(89)81177-9