scholarly journals Construction of transducing phage .RHO.11 containing .ALPHA.-amylase structural gene of Bacillus subtilis.

1979 ◽  
Vol 43 (12) ◽  
pp. 2637-2638 ◽  
Author(s):  
S. NOMURA ◽  
K. YAMANE ◽  
T. MASUDA ◽  
F. KAWAMURA ◽  
T. MIZUKAMI ◽  
...  
1983 ◽  
Vol 47 (1) ◽  
pp. 159-161 ◽  
Author(s):  
Yasutoshi TAKEICHI ◽  
Kazutaka OHMURA ◽  
Akira NAKAYAMA ◽  
Kiyotaka OTOZAI ◽  
Kunio YAMANE

2014 ◽  
Vol 8 (21) ◽  
pp. 2168-2173 ◽  
Author(s):  
Aygan Ashabil ◽  
Sariturk Sevtap ◽  
Kostekci Sedat ◽  
Tanis Huseyin

1975 ◽  
Vol 121 (2) ◽  
pp. 688-694 ◽  
Author(s):  
J Sekiguchi ◽  
N Takada ◽  
H Okada

1974 ◽  
Vol 128 (3) ◽  
pp. 213-221 ◽  
Author(s):  
J. -A. Lepesant ◽  
J. Lepesant-Kejzlarová ◽  
M. Pascal ◽  
F. Kunst ◽  
A. Billault ◽  
...  

2008 ◽  
Vol 78 (1) ◽  
pp. 85-94 ◽  
Author(s):  
Yi-han Liu ◽  
Fu-ping Lu ◽  
Yu Li ◽  
Xiang-bin Yin ◽  
Yi Wang ◽  
...  

1983 ◽  
Vol 209 (2) ◽  
pp. 561-564 ◽  
Author(s):  
A R Orlando ◽  
P Ade ◽  
D Di Maggio ◽  
C Fanelli ◽  
L Vittozzi

A new alpha-amylase (EC 3.2.1.1) from Bacillus subtilis was purified by affinity chromatography. The molecular weight of the purified enzyme, estimated from sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, was 93000, which is very different from the molecular weights of two well-characterized amylases from B. subtilis. Electrofocusing showed an isoelectric point of 5. Amylase shows a broad maximum of activity between pH 6 and 7; maximal inhibition of enzyme by wheat-protein alpha-amylase inhibitors is displayed at pH 7.


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