scholarly journals Purification and properties of alanine dehydrogenase from Bacillus natto KMD 1126.

1977 ◽  
Vol 25 (8) ◽  
pp. 2061-2066 ◽  
Author(s):  
KATSUHIKO MATSUI ◽  
YUKIKO TAMEGAI ◽  
AKIKO MIYANO ◽  
YUKIO KAMEDA
1977 ◽  
Vol 25 (4) ◽  
pp. 761-766 ◽  
Author(s):  
KATSUHIKO MATSUI ◽  
YUKIO KAMEDA ◽  
TAKUMI ATSUSAKA ◽  
MINAKO HIGAKI ◽  
KEIKO SASAKI

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 ◽  
...  

1973 ◽  
Vol 21 (3) ◽  
pp. 538-545
Author(s):  
YUKIO KAMEDA ◽  
KATSUHIKO MATSUI ◽  
KAZUYOSHI HOSOYA ◽  
AKIRA NOMURA ◽  
NORIKO SUGANO

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