scholarly journals Preliminary Characterization of Cell-free K99 Antigen Isolated from Escherichia coli B41

1977 ◽  
Vol 99 (2) ◽  
pp. 353-357 ◽  
Author(s):  
J. A. Morris ◽  
A. E. Stevens ◽  
W. J. Sojka
1992 ◽  
Vol 283 (2) ◽  
pp. 327-331 ◽  
Author(s):  
O Ploux ◽  
A Marquet

The 8-amino-7-oxopelargonate synthase [6-carboxyhexanoyl-CoA:L-alanine carboxyhexanoyltransferase (decarboxylating); EC 2.3.1.47] from Bacillus sphaericus involved in biotin biosynthesis was purified from an Escherichia coli overproducing strain. The purification afforded an electrophoretically homogeneous enzyme with a specific activity of 0.67 unit/mg. The purified enzyme is a monomer of 41 kDa. N-Terminal sequencing of the first 14 amino acid residues showed complete agreement with the predicted sequence from the bioF gene. The pure enzyme showed the characteristic absorption band (425 nm) of pyridoxal 5′-phosphate-dependent enzymes. Furthermore, the holoenzyme was resolved during an affinity step yielding the inactive apoenzyme, which recovered activity and the 425 nm-absorption band on dialysis against pyridoxal 5′-phosphate. Km values for L-alanine and pimeloyl-CoA were respectively 3 mM and 1 microM.


2003 ◽  
Vol 28 (1) ◽  
pp. 78-85 ◽  
Author(s):  
Camilla Giammarini ◽  
Francesca Andreoni ◽  
Giulia Amagliani ◽  
Annarita Casiere ◽  
Simone Barocci ◽  
...  

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