ENGINEERING RESISTANCE TO TRYPSIN INACTIVATION INTO L-ASPARAGINASE THROUGH THE PRODUCTION OF A CHIMERIC PROTEIN BETWEEN THE ENZYME AND A PROTECTIVE SINGLE-CHAIN ANTIBODY

Authors
NEWSTED WJ RAMJEESINGH M ZYWULKO M ROTHSTEIN SJ SHAMI EY
Citation
Wj. Newsted et al., ENGINEERING RESISTANCE TO TRYPSIN INACTIVATION INTO L-ASPARAGINASE THROUGH THE PRODUCTION OF A CHIMERIC PROTEIN BETWEEN THE ENZYME AND A PROTECTIVE SINGLE-CHAIN ANTIBODY, Enzyme and microbial technology, 17(8), 1995, pp. 757-764
Citations number
22
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
Enzyme and microbial technology → ACNP
ISSN journal
01410229
Volume
17
Issue
8
Year of publication
1995
Pages
757 - 764
Database
ISI
SICI code
0141-0229(1995)17:8<757:ERTTII>2.0.ZU;2-Q
Abstract
We have demonstrated that a trypsin sensitive enzyme such as L-asparag inase can be rendered trypsin resistant by genetically fusing its gene with that of a single-chain antibody derived from a preselected monoc lonal antibody capable of providing protection against trypsin. The ch imeric L-asparaginase retained 75% of its original activity upon expos ure to trypsin, whereas the native unprotected L-asparaginase control was totally inactivated.