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 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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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. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(89)81177-9 |