Barley malt-α-amylase. Purication, action pattern, and subsite mapping of isozyme 1 and two members of the isozyme 2 subfamily using p-nitrophenylated maltooligosaccharide substrates-Reference-Cited by-同舟云学术

Barley malt-α-amylase. Purication, action pattern, and subsite mapping of isozyme 1 and two members of the isozyme 2 subfamily using p-nitrophenylated maltooligosaccharide substrates

Published:1992-09 Issue:2 Volume:1159 Page:193-202
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Ajandouz El Hassan,Abe Jun-ichi,Svensson Birte,Marchis-Mouren Guy

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference38 articles.

1. Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 A resolution. Role of calcium in structure and activity.

2. Structure and Possible Catalytic Residues of Taka-Amylase A

3. Calcium binding in .alpha.-amylases: an x-ray diffraction study at 2.1-.ANG. resolution of two enzymes from Aspergillus

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