scholarly journals Purification and characterization of a prokaryotic glycoprotein from the cell envelope of Halobacterium salinarium.

1976 ◽  
Vol 251 (7) ◽  
pp. 2005-2014 ◽  
Author(s):  
M F Mescher ◽  
J L Strominger
Keyword(s):  
Cell Envelope ◽  
Halobacterium Salinarium ◽  
Purification And Characterization

scholarly journals Purification and Characterization of the Bacterial UDP-GlcNAc:Undecaprenyl-Phosphate GlcNAc-1-Phosphate Transferase WecA

2008 ◽  
Vol 190 (21) ◽  
pp. 7141-7146 ◽  
Author(s):  
Bayan Al-Dabbagh ◽  
Dominique Mengin-Lecreulx ◽  
Ahmed Bouhss
Keyword(s):  
Cell Envelope ◽  
Functional Characterization ◽  
Integral Membrane Protein ◽  
Minimal Length ◽  
Purification And Characterization ◽  
Effects Of Ph ◽  
Undecaprenyl Phosphate ◽  
First Time ◽  
Lipid Substrate

ABSTRACT To date, the structural and functional characterization of proteins belonging to the polyprenyl-phosphate N-acetylhexosamine-1-phosphate transferase superfamily has been relentlessly held back by problems encountered with their overexpression and purification. In the present work and for the first time, the integral membrane protein WecA that catalyzes the transfer of the GlcNAc-1-phosphate moiety from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-GlcNAc, the lipid intermediate involved in the synthesis of various bacterial cell envelope components, was overproduced and purified to near homogeneity in milligram quantities. An enzymatic assay was developed, and the kinetic parameters of WecA as well as the effects of pH, salts, cations, detergents, and temperature on the enzyme activity were determined. A minimal length of 35 carbons was required for the lipid substrate, and tunicamycin was shown to inhibit the enzyme at submicromolar concentrations.

Purification and characterization of phosphoglucomutase from peas

1994 ◽  
Vol 92 (3) ◽  
pp. 479-486 ◽  
Author(s):  
Cynthia M. Galloway ◽  
W. Mack Dugger
Keyword(s):  
Purification And Characterization
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