scholarly journals Studies on the primary structure of .ALPHA.-amylase from Bacillus subtilis var. amylosacchariticus. Part IV. Alignments of tryptic peptides in CNBr fragments of .ALPHA.-amylase from Bacillus subtilis var. amylosacchariticus.

1985 ◽  
Vol 49 (7) ◽  
pp. 1933-1942
Author(s):  
Yoshiho NAGATA
1980 ◽  
Vol 185 (2) ◽  
pp. 387-395 ◽  
Author(s):  
H Chung ◽  
F Friedberg

Bacillus amyloliquefaciens alpha-amylase (1,4-alpha-D-glucan glucanohydrolase. EC 3.2.1.1), which is commercially supplied as ‘Bacillus subtilis alpha-amylase’ does not cross-react immunologically with B. subtilis alpha-amylase. This enzyme (from B. amyloliquefaciens) was cleaved by treatment with CNBr into seven fragments. Peptide A was selected for sequence determination. It is the longest one, containing 185 amino acids (i.e. approx. 50% of the total molecule) and connects to the hexapeptide of the N-terminus. Its primary structure was aligned by use of various proteolytic enzymes. The sequence of amino acids 181-184 is identical with that of amino acids 14-17 of the alpha-amylase isolated from B. subtilis (except that amino acid 183 is asparagine rather than aspartic acid).


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

1983 ◽  
Vol 47 (1) ◽  
pp. 159-161 ◽  
Author(s):  
Yasutoshi TAKEICHI ◽  
Kazutaka OHMURA ◽  
Akira NAKAYAMA ◽  
Kiyotaka OTOZAI ◽  
Kunio YAMANE

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