Novel affinity chromatography method for the efficient purification of recombinant Binder of SPerm homolog proteins
Corresponding Author
Samin Sabouhi Zarafshan
Maisonneuve-Rosemont Hospital Research Centre, Montreal, Quebec, Canada
Department of Biochemistry and Molecular Medicine, Faculty of Medicine, University of Montreal, Montreal, Quebec, Canada
Correspondence
Samin Sabouhi Zarafshan, Centre de Recherche de l'Hôpital Maisonneuve-Rosemont, 5415 boulevards de L'Assomption, Montreal, Quebec, Canada, H1T 2M4
Email: [email protected]
Puttaswamy Manjunath
Email: [email protected]
Search for more papers by this authorCorresponding Author
Puttaswamy Manjunath
Maisonneuve-Rosemont Hospital Research Centre, Montreal, Quebec, Canada
Department of Biochemistry and Molecular Medicine, Faculty of Medicine, University of Montreal, Montreal, Quebec, Canada
Correspondence
Samin Sabouhi Zarafshan, Centre de Recherche de l'Hôpital Maisonneuve-Rosemont, 5415 boulevards de L'Assomption, Montreal, Quebec, Canada, H1T 2M4
Email: [email protected]
Puttaswamy Manjunath
Email: [email protected]
Search for more papers by this authorCorresponding Author
Samin Sabouhi Zarafshan
Maisonneuve-Rosemont Hospital Research Centre, Montreal, Quebec, Canada
Department of Biochemistry and Molecular Medicine, Faculty of Medicine, University of Montreal, Montreal, Quebec, Canada
Correspondence
Samin Sabouhi Zarafshan, Centre de Recherche de l'Hôpital Maisonneuve-Rosemont, 5415 boulevards de L'Assomption, Montreal, Quebec, Canada, H1T 2M4
Email: [email protected]
Puttaswamy Manjunath
Email: [email protected]
Search for more papers by this authorCorresponding Author
Puttaswamy Manjunath
Maisonneuve-Rosemont Hospital Research Centre, Montreal, Quebec, Canada
Department of Biochemistry and Molecular Medicine, Faculty of Medicine, University of Montreal, Montreal, Quebec, Canada
Correspondence
Samin Sabouhi Zarafshan, Centre de Recherche de l'Hôpital Maisonneuve-Rosemont, 5415 boulevards de L'Assomption, Montreal, Quebec, Canada, H1T 2M4
Email: [email protected]
Puttaswamy Manjunath
Email: [email protected]
Search for more papers by this authorAbstract
In mammalian species, a family of proteins named the Binder of SPerm proteins, which are expressed in the male reproductive tract, have been shown to play a role in epididymal sperm maturation and sperm capacitation. Recently, one homolog from human and two homologs from mouse were characterized. In order to further investigate the biochemical activity of these proteins, efficient purification procedures are required to isolate the proteins. Since these proteins are produced in very minute quantities, we exploited the high capacity of Escherichia coli to produce larger quantities of recombinant proteins that were subsequently purified using affinity chromatography on a diethylaminoethyl-Sephadex A-25 column. Binder of SPerm proteins have been shown to interact with pseudo-choline groups such as diethylaminoethyl through affinity rather than ionic interactions. The aim of the current study was to develop a novel method for purifying these recombinant proteins, produced in Escherichia coli cells. Diethylaminoethyl is positively charged and is a weak anion exchanger, but binder of sperm proteins interacts with affinity to this resin. This study presents a new, rapid, and cost-effective purification method that provides with an exceptional purity level, which can be used to study their roles in mammalian fertilization.
CONFLICT OF INTEREST
The authors have declared no conflict of interest.
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