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 ◽  
...  

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.

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

1995 ◽  
Vol 6 (3) ◽  
pp. 251-255 ◽  
Author(s):  
U. Treichel ◽  
T. Schreiter ◽  
K.H.M. Zumbuschenfelde ◽  
R.J. Stockert

2020 ◽  
Author(s):  
Aiping Wang ◽  
Jiaoyue Han ◽  
Rui Jia ◽  
Jingming Zhou ◽  
Hongliang Liu ◽  
...  

1985 ◽  
Vol 228 (3) ◽  
pp. 627-634 ◽  
Author(s):  
R K Scopes ◽  
V Testolin ◽  
A Stoter ◽  
K Griffiths-Smith ◽  
E M Algar

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.


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