Purification and Characterization of Human Pancreatic Polypeptide Expressed in E. coli

1995 ◽  
Vol 213 (1) ◽  
pp. 239-248
Author(s):  
Y.V. Griko ◽  
M.D. Kapanadze
2007 ◽  
Vol 55 (2) ◽  
pp. 312-318 ◽  
Author(s):  
Ziyong Sun ◽  
Wei Lu ◽  
Yanchun Tang ◽  
Jing Zhang ◽  
Junyong Chen ◽  
...  

1978 ◽  
Vol 169 (3) ◽  
pp. 633-641 ◽  
Author(s):  
S A Baldwin ◽  
R N Perham ◽  
D Stribling

A new form of the class-II D-fructose 1,6-bisphosphate aldolase (EC 4.1.2.13) of Escherichia coli (Crookes' strain) was isolated from an extract of glycerol-grown bacteria. It has a higher molecular weight (approx. 80000)than previous preparations of the enzyme and closely resembles the typical class-II aldolase from yeast in size and amino acid composition. On the other hand, its kinetic behaviour is not typical of a class-II aldolase. The enzyme has no requirement for thiol compounds either for stability or activity, added K+ ions have no effect, and the optimum pH for the cleavage activity is unusually high. The class-II enzymes from the prokaryote E. coli and the eukaryote yeast show no immunological identity. However, the similarity of their structures suggests that they have evolved from a common ancestor.


2009 ◽  
Vol 25 ◽  
pp. S293-S294
Author(s):  
M.C.D.S. Pranchevicius ◽  
L. Oliveira ◽  
N.C. Avanci ◽  
J.C. Rosa ◽  
A.C. Quiapim ◽  
...  

2004 ◽  
Vol 36 (2) ◽  
pp. 118-122 ◽  
Author(s):  
Xiao-Xia Xia ◽  
Ya-Ling Shen ◽  
Dong-Zhi Wei

Abstract As a potential anti-tumor protein, tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) has drawn considerable attention. This report presented the purification and characterization of soluble TRAIL, expressed as inclusion bodies in E. coli. sTRAIL inclusion bodies were solubilized and refolded at a high concentration up to 0.9 g/L by a simple dilution method. Refolded protein was purified to electrophoretic homogeneity by a single-step immobilized metal affinity chromatography. The purified sTRAIL had a strong cytotoxic activity against human pancreatic tumor cell line 1990, with ED50 about 1.5 mg/L. Circular dichroism and fluorescence spectrum analysis showed that the refolded sTRAIL had a structure similar to that of native protein with β-sheet secondary structure. This efficient procedure of sTRAIL renaturation may be useful for the mass production of this therapeutically important protein.


Biochemistry ◽  
1982 ◽  
Vol 21 (13) ◽  
pp. 3064-3069 ◽  
Author(s):  
Chandra M. Dwivedi ◽  
Richard C. Ragin ◽  
Jack R. Uren

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