Porcine pancreatic α-amylase: a model for structure—function studies of homodepolymerases
- 30 September 1988
- Vol. 70 (9) , 1163-1170
- https://doi.org/10.1016/0300-9084(88)90181-2
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- The determination of subsite binding energies of porcine pancreatic α-amylase by comparing hydrolytic activity towards substratesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- Comparison of amino acid sequences of eleven different ?-amylasesApplied Microbiology and Biotechnology, 1986
- Complete amino acid sequence and location of the five disulfide bridges in porcine pancreatic α-amylaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Structure and Possible Catalytic Residues of Taka-Amylase AThe Journal of Biochemistry, 1984
- Amino acid sequence of hog pancreatic α‐amylase isoenzyme IFEBS Letters, 1981
- The three-dimensional structure of α-amylase from porcine pancreas at 5 Å resolution – the active-site locationActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1980
- Identity and properties of the chloride effector binding site in hog pancreatic α-amylaseBiochemistry, 1976
- The Allosteric Activation of Mammalian α‐Amylase by ChlorideEuropean Journal of Biochemistry, 1974
- Characterization of Porcine Pancreatic Isoamylases Chemical and Physical StudiesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1970
- Alpha-Amylases as Calcium-Metalloenzymes. I. Preparation of Calcium-free Apoamylases by Chelation and Electrodialysis*Biochemistry, 1964