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Title 

Maltose binding protein(MBP) fusion proteins with low or no affinity to amylose resins can be single-step purified using a novel anti-MBP monoclonal antibody

Authors 

Jung Hyun ParkEun A ChoiEun Wie ChoKyung Soo HahmKil Lyong Kim

Publisher 

Springer Verlag (Germany)

Issue Date 

1998

Citation 

Molecules and Cells, vol. 8, no. 6, pp. 709-716

Keywords 

Maltose Binding ProteinMonoclonal AntibodyProtein Purification

Abstract 

The maltose binding protein (MBP) fusion protein expression system is a powerful tool to produce and isolate recombinant proteins in E. coli. Whereas the conventional isolation technique for MBP-fusion proteins takes advantage of the binding affinity of MBP to maltose, this method is limited insofar as the biological activity of MBP has to be fully conserved for a successful purification. In this study, a novel monoclonal antibody (mAb) specific for MBP, termed HAM-19, was generated and its application in the purification and detection of MBP-fusion proteins determined. Using anti-MBP immunoaffintiy columns, even recombinant MBP fusion products with lowered or impaired binding affinity to maltose were purified in a single step procedure. In comparison to amylose resins, HAM-19 immunoaffinity columns showed a higher binding capacity and affinity to MBP-fusion proteins. Furthermore, the mAb HAM-19 also provides a technical improvement over polyclonal antisera for the detection and analysis of MBP-fusion proteins which are under use in various forms in the fields of molecular and cellular biology.

ISSN 

1016-8478

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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