A Novel Thermostability Conferring Property of Cherry
Tag and its Application in Purification of Fusion Proteins |
Krishna Mohan Padmanabha Das, Shruti Barve,
Sampali Banerjee,
Suman Bandyopadhyay and Sriram Padmanabhan* |
| Lupin Limited, Biotech R & D, Gat #1156 Ghotawade Village, Mulshi Taluka, Pune-411042, India |
| *Corresponding author: |
Dr. Sriram Padmanabhan,
Director, Biotechnology
R & D Lupin Limited,
Gat #1156, Ghotawade Village,
Mulshi
Taluka,
Pune-411042, India,
Tel: + 91-20-66549801,
Fax: + 91-20-
66549807,
E-mail: srirampadmanabhan@lupinpharma.com |
|
| Received December 08, 2009; Accepted December 26, 2009; Published December 26, 2009 |
Citation: Das KMP, Barve S, Banerjee S, Bandyopadhyay S, Padmanabhan S (2009) A Novel Thermostability Conferring Property of Cherry Tag and its Application in Purification of Fusion Proteins. J Microbial Biochem Technol 1: 059-063. doi:10.4172/1948-5948.1000012 |
Copyright: © 2009 Das KMP, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution
License,which permits unrestricted use, distribution, and reproduction
in any medium, provided the original author and source are credited. |
| Abstract |
Cherry tag, a red polypeptide of the heme binding part
of cytochrome is used to attain high levels of soluble protein
expression in E. coli. A novel heat stability conferring
property of this tag was observed and studied for constructs
of two soluble fusions especially Cherry-Granulocyte
colony stimulating factor (GCSF) and Cherry-
Staphylokinase (SAK). Heat incubation of these fusion
proteins at 70oC for 20 minutes culminated in specific
denaturation and precipitation of E. coli proteins excluding
the fusion proteins. Both the heat treated fusion proteins
were found to be functionally active. Thus Cherry
fusion tag could be used as a cost-efficient tool in purification
of proteins by imparting heat stability. |
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