Intermediate metabolism of aerobic spores. V. The purification and properties of l-alanine dehydrogenase

1960 ◽  
Vol 91 (2) ◽  
pp. 290-299 ◽  
Author(s):  
R.J. O'Connor ◽  
H.O. Halvorson
1977 ◽  
Vol 25 (8) ◽  
pp. 2061-2066 ◽  
Author(s):  
KATSUHIKO MATSUI ◽  
YUKIKO TAMEGAI ◽  
AKIKO MIYANO ◽  
YUKIO KAMEDA

1957 ◽  
Vol 73 (4) ◽  
pp. 470-476 ◽  
Author(s):  
Brooks D. Church ◽  
Harlyn Halvorson

1959 ◽  
Vol 78 (6) ◽  
pp. 844-851 ◽  
Author(s):  
Richard O'Connor ◽  
Harlyn Halvorson

1959 ◽  
Vol 77 (1) ◽  
pp. 43-54 ◽  
Author(s):  
Roy Doi ◽  
Harlyn Halvorson ◽  
Brooks Church

1977 ◽  
Vol 161 (2) ◽  
pp. 313-320 ◽  
Author(s):  
E K Kim ◽  
P S Fitt

1. Halobacterium cutirubrum L-alanine dehydrogenase was purified approx. 100-fold. 2. It has a mol. wt. of 72 500, about one-third that of two well-studied alanine dehydrogenases from non-halophiles. 3. The activity of the enzyme increases with temperature up to 70 degrees C, but the protein itself is not thermostable. 4. In the reductive amination reaction, the enzyme is fully active in the presence of high concentrations of K+, Na+ or NH4+ and partially active with Cs+ or Li+, but for oxidative deamination it has an absolute requirement for K+.


1989 ◽  
Vol 179 (1) ◽  
pp. 221-227 ◽  
Author(s):  
Ales VANCURA ◽  
Ivana VANCUROVA ◽  
Jindrich VOLC ◽  
Shanagh K. T. JONES ◽  
Miroslav FLIEGER ◽  
...  

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