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פותח על ידי קלירמאש פתרונות בע"מ -
Isolation of fusion proteins containing SecY and SecE, components of the protein translocation complex from the halophilic archaeon Haloferax volcanii
Year:
2003
Source of publication :
Extremophiles
Authors :
יריחימוביץ', ורד
;
.
Volume :
7
Co-Authors:
Irihimovitch, V., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel
Ring, G., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel
Elkayam, T., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel
Konrad, Z., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel
Eichler, J., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel
Facilitators :
From page:
71
To page:
77
(
Total pages:
7
)
Abstract:
By exploiting the salt-insensitive interaction of the cellulose-binding domain (CBD) of the Clostridium thermocellum cellulosome with cellulose, purification of CBD-fused versions of SecY and SecE, components of the translocation apparatus of the halophilic archaeon Haloferax volcanii, was undertaken. Following transformation of Haloferax volcanii cells with CBD-SecY- or -SecE-encoding plasmids, cellulose-based purification led to the capture of stably expressed, membrane-bound 68 and 25 kDa proteins, respectively. Both fusion proteins were recognized by antibodies raised against the CBD. Thus, CBD-cellulose interactions can be employed as a salt-insensitive affinity purification system for the capture of complexes containing the Haloferax volcanii translocation apparatus components SecY and SecE. © Springer-Verlag 2002.
Note:
Related Files :
Base Sequence
chemistry
Clostridium thermocellum
Gene
gene expression
Genetics
Halophiles
SecE protein, E coli
עוד תגיות
תוכן קשור
More details
DOI :
10.1007/s00792-002-0297-0
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
22793
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:54
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Scientific Publication
Isolation of fusion proteins containing SecY and SecE, components of the protein translocation complex from the halophilic archaeon Haloferax volcanii
7
Irihimovitch, V., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel
Ring, G., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel
Elkayam, T., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel
Konrad, Z., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel
Eichler, J., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel
Isolation of fusion proteins containing SecY and SecE, components of the protein translocation complex from the halophilic archaeon Haloferax volcanii
By exploiting the salt-insensitive interaction of the cellulose-binding domain (CBD) of the Clostridium thermocellum cellulosome with cellulose, purification of CBD-fused versions of SecY and SecE, components of the translocation apparatus of the halophilic archaeon Haloferax volcanii, was undertaken. Following transformation of Haloferax volcanii cells with CBD-SecY- or -SecE-encoding plasmids, cellulose-based purification led to the capture of stably expressed, membrane-bound 68 and 25 kDa proteins, respectively. Both fusion proteins were recognized by antibodies raised against the CBD. Thus, CBD-cellulose interactions can be employed as a salt-insensitive affinity purification system for the capture of complexes containing the Haloferax volcanii translocation apparatus components SecY and SecE. © Springer-Verlag 2002.
Scientific Publication
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