High-Yield Expression, Purification, and Characterization of Active, SolubleBacteroides fragilisMetallo-β-Lactamase, CcrA

1997 ◽  
Vol 9 (3) ◽  
pp. 355-362 ◽  
Author(s):  
Jeffrey H. Toney ◽  
Joseph K. Wu ◽  
Karen M. Overbye ◽  
Chris M. Thompson ◽  
David L. Pompliano
Keyword(s):  
High Yield ◽  
Purification And Characterization

High-yield purification and characterization of recombinant human leukotactin-1 inPichia pastoris

2004 ◽  
Vol 9 (1) ◽  
pp. 1-6 ◽  
Author(s):  
In Hwan Lim ◽  
Kong Ju Lee ◽  
Eun Kyoung Lee ◽  
Mu Rim Choi ◽  
Gue-Wha Lee ◽  
...  
Keyword(s):  
High Yield ◽  
Purification And Characterization

High-Yield Purification and Characterization of Human Asialoglycoprotein Receptor

1995 ◽  
Vol 6 (3) ◽  
pp. 251-255 ◽  
Author(s):  
U. Treichel ◽  
T. Schreiter ◽  
K.H.M. Zumbuschenfelde ◽  
R.J. Stockert
Keyword(s):  
Asialoglycoprotein Receptor ◽  
High Yield ◽  
Purification And Characterization

scholarly journals Simultaneous purification and characterization of glucokinase, fructokinase and glucose-6-phosphate dehydrogenase from Zymomonas mobilis

1985 ◽  
Vol 228 (3) ◽  
pp. 627-634 ◽  
Author(s):  
R K Scopes ◽  
V Testolin ◽  
A Stoter ◽  
K Griffiths-Smith ◽  
E M Algar
Keyword(s):  
Kinetic Parameters ◽  
Zymomonas Mobilis ◽  
High Yield ◽  
Purification And Characterization ◽  
Glucose 6 Phosphate Dehydrogenase

The three enzymes glucokinase (EC 2.7.1.2), fructokinase (EC 2.7.1.4) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) were isolated in high yield from extracts of Zymomonas mobilis. The principal steps in the isolation procedures involved the use of selected dye-ligand adsorbent columns, with affinity elution of two of the three enzymes. Glucokinase and fructokinase are dimeric proteins (2 × 33000 Da and 2 × 28000 Da respectively) and glucose-6-phosphate dehydrogenase is a tetramer (4 × 52000 Da). Some similarities in the structural and kinetic parameters of the two kinases were noted, but they have absolute specificity for their substrates. Fructokinase is strongly inhibited by glucose; otherwise non-substrate sugars had little effect on any of the three enzymes.

High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h 2

2003 ◽  
Vol 31 (2) ◽  
pp. 250-259 ◽  
Author(s):  
Katrin Lehmann ◽  
Silke Hoffmann ◽  
Philipp Neudecker ◽  
Martin Suhr ◽  
Wolf-Meinhard Becker ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
High Yield ◽  
Purification And Characterization ◽  
Peanut Allergen ◽  
Ara H 2 ◽  
Expression In Escherichia Coli

High-yield expression, purification and characterization of tumor-targeted IFN-α2a

Cytotherapy ◽  
2007 ◽  
Vol 9 (1) ◽  
pp. 60-68 ◽  
Author(s):  
J. Meng ◽  
Z. Yan ◽  
J. Wu ◽  
L. Li ◽  
X. Xue ◽  
...  
Keyword(s):  
High Yield ◽  
Purification And Characterization

scholarly journals Heterologous Expression, Purification, and Characterization of a Highly Active Xylose Reductase from Neurospora crassa

2005 ◽  
Vol 71 (3) ◽  
pp. 1642-1647 ◽  
Author(s):  
Ryan Woodyer ◽  
Michael Simurdiak ◽  
Wilfred A. van der Donk ◽  
Huimin Zhao
Keyword(s):  
Neurospora Crassa ◽  
Xylose Reductase ◽  
Whole Genome Sequence ◽  
High Yield ◽  
In Vitro Production ◽  
Purification And Characterization ◽  
Highly Active ◽  
Vitro Production

ABSTRACT A xylose reductase (XR) gene was identified from the Neurospora crassa whole-genome sequence, expressed heterologously in Escherichia coli, and purified as a His6-tagged fusion in high yield. This enzyme is one of the most active XRs thus far characterized and may be used for the in vitro production of xylitol.

scholarly journals Highly efficient soluble expression, purification and characterization of recombinant Aβ42 fromEscherichia coli

RSC Advances ◽  
2018 ◽  
Vol 8 (33) ◽  
pp. 18434-18441 ◽  
Author(s):  
Longgang Jia ◽  
Wenjuan Wang ◽  
Jinzhao Shang ◽  
Wenping Zhao ◽  
Wei Wei ◽  
...  
Keyword(s):  
Cleavage Site ◽  
Maltose Binding Protein ◽  
Tobacco Etch Virus ◽  
Soluble Expression ◽  
High Yield ◽  
Expression And Purification ◽  
Purification And Characterization ◽  
Purification Method ◽  
Fromescherichia Coli

A novel high-yield expression and purification method for Aβ42 based on a fusion with maltose binding protein followed by the soluble polypeptide linker (NANP)3and a modified tobacco etch virus cleavage site before the Aβ42 was developed.

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