Bovine Acetylcholinestrase — Cloning, Expression and Characterization of the Recombinant Enzyme

Author(s):  
Itai Mendelson ◽  
Chanoh Kronman ◽  
Nechama Zeliger ◽  
Tamar Seri ◽  
Arie Ordentlich ◽  
...  
Keyword(s):  
1993 ◽  
Vol 268 (7) ◽  
pp. 4832-4838 ◽  
Author(s):  
D. Brömme ◽  
P.R. Bonneau ◽  
P. Lachance ◽  
B. Wiederanders ◽  
H. Kirschke ◽  
...  

Biochemistry ◽  
2001 ◽  
Vol 40 (49) ◽  
pp. 14847-14854 ◽  
Author(s):  
Tim Soderberg ◽  
Anjun Chen ◽  
C. Dale Poulter

2007 ◽  
Vol 73 (9) ◽  
pp. 3109-3112 ◽  
Author(s):  
Tatsuji Sakamoto ◽  
Yuya Taniguchi ◽  
Shiho Suzuki ◽  
Hideshi Ihara ◽  
Haruhiko Kawasaki

ABSTRACT A type II arabinogalactan-degrading enzyme (FoGal1) was purified from Fusarium oxysporum 12S, and the corresponding cDNA was isolated. FoGal1 had high similarity to enzymes of glycoside hydrolase family 5. Treatment of larch wood arabinogalactan with the recombinant enzyme indicated that FoGal1 is a β-1,6-galactanase that preferentially debranches β-1,6-galactobiose from the substrate.


FEBS Letters ◽  
1999 ◽  
Vol 455 (1-2) ◽  
pp. 13-17 ◽  
Author(s):  
Monica Emanuelli ◽  
Francesco Carnevali ◽  
Maria Lorenzi ◽  
Nadia Raffaelli ◽  
Adolfo Amici ◽  
...  

1992 ◽  
Vol 284 (3) ◽  
pp. 749-754 ◽  
Author(s):  
G McAllister ◽  
P Whiting ◽  
E A Hammond ◽  
M R Knowles ◽  
J R Atack ◽  
...  

Inositol monophosphatase (EC 3.1.3.25) is a key enzyme in the phosphoinositide cell-signalling system. Its role is to provide inositol required for the resynthesis of phosphatidylinositol and polyphosphoinositides. It is the probable pharmacological target for lithium action in brain. Using probes derived from the bovine inositol monophosphatase cDNA we have isolated cDNA clones encoding the human and rat brain enzymes. The enzyme is highly conserved in all three species (79% identical). The coding region of the human cDNA was inserted into a bacterial expression vector. The expressed recombinant enzyme was purified and its biochemical properties examined. The human enzyme is very similar to the bovine enzyme.


1999 ◽  
Vol 181 (8) ◽  
pp. 2323-2329 ◽  
Author(s):  
Miguel Prudêncio ◽  
Robert R. Eady ◽  
Gary Sawers

ABSTRACT The nirA gene encoding the blue dissimilatory nitrite reductase from Alcaligenes xylosoxidans has been cloned and sequenced. To our knowledge, this is the first report of the characterization of a gene encoding a blue copper-containing nitrite reductase. The deduced amino acid sequence exhibits a high degree of similarity to other copper-containing nitrite reductases from various bacterial sources. The full-length protein included a 24-amino-acid leader peptide. The nirA gene was overexpressed inEscherichia coli and was shown to be exported to the periplasm. Purification was achieved in a single step, and analysis of the recombinant Nir enzyme revealed that cleavage of the signal peptide occurred at a position identical to that for the native enzyme isolated from A. xylosoxidans. The recombinant Nir isolated directly was blue and trimeric and, on the basis of electron paramagnetic resonance spectroscopy and metal analysis, possessed only type 1 copper centers. This type 2-depleted enzyme preparation also had a low nitrite reductase enzyme activity. Incubation of the periplasmic fraction with copper sulfate prior to purification resulted in the isolation of an enzyme with a full complement of type 1 and type 2 copper centers and a high specific activity. The kinetic properties of the recombinant enzyme were indistinguishable from those of the native nitrite reductase isolated from A. xylosoxidans. This rapid isolation procedure will greatly facilitate genetic and biochemical characterization of both wild-type and mutant derivatives of this protein.


2002 ◽  
Vol 7 (7) ◽  
pp. 639-651 ◽  
Author(s):  
Noriko Shimazaki ◽  
Kenta Yoshida ◽  
Toshiko Kobayashi ◽  
Shingo Toji ◽  
Katsuyuki Tamai ◽  
...  

1998 ◽  
Vol 37 (1) ◽  
pp. 39-43 ◽  
Author(s):  
Lam-Son Phan Trân ◽  
Lóránd Szabó ◽  
László Fülöp ◽  
László Orosz ◽  
Tibor Sík ◽  
...  

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