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Title 

Single-step purification of proteins of interest from proteolytically cleaved recombinant maltose-binding protein (MBP) fusion proteins by selective immunoprecipitation of MBP

Authors 

Jung Hyun ParkShin Young NaDong Gun LeeByoung Don HanKil Lyong Kim

Publisher 

Springer Verlag (Germany)

Issue Date 

1998

Citation 

Biotechnology and Bioprocess Engineering, vol. 3, no. 0, pp. 82-86

Keywords 

maltose binding protein (MBP)factor Xarecombinant proteinprotein purificationanti-MBP monoclonal antibody

Abstract 

The maltose binding protein (MBP) fusion protein system is a versatile tool to express and isolate recombinant proteins in E. coli. In this system, MBP fusion proteins are efficiently isolated from whole cell lysate using amylose conjugated agarose beads and then eluted by competition with free maltose. Since MBP is a rather large molecule (∼42 kDa), for further experiments, the MBP part is usually proteolytically cleaved from the fusion protein and subsequently removed by ion-exchange chromatography or rebinding to amylose columns after washing out excess and MBP-bound maltose. In the present study, we have developed an improved method for the removal of cleaved MBP, which is advantageous over conventional methods. In this method, factor Xa cleaved MBP fusion proteins were incubated with Sepharose beads conjugated with MBP specific monoclonal antibodies and then precipitated by centrifugation, resulting in highly purified proteins in the supernatant.

ISSN 

1226-8372

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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