TY - JOUR
T1 - Ostrich pancreatic α-amylase
T2 - Kinetic properties, amino terminal sequence and subsite structure
AU - Oosthuizen, Vaughan
AU - Naudé, Ryno J.
AU - Oelofsen, Willem
AU - Koji, Muramoto
AU - Hisao, Kamiya
PY - 1994/1/1
Y1 - 1994/1/1
N2 - Ostrich pancreatic α-amylase (OPA) was purified to homogeneity in the presence of protease inhibitors by a single-step affinity chromatography technique. The first 53 amino acids of the N-terminus were identified by gas-phase sequencing. From kinetic parameters (kcat/Km) a subsite profile was established leading to a five subsite model for OPA. The pKa values of catalytic residues were determined as 5.75 and 8.36. Inhibition of OPA by monosaccharides, β-cyclodextrin and a wheat α-amylase inhibitor was studied.
AB - Ostrich pancreatic α-amylase (OPA) was purified to homogeneity in the presence of protease inhibitors by a single-step affinity chromatography technique. The first 53 amino acids of the N-terminus were identified by gas-phase sequencing. From kinetic parameters (kcat/Km) a subsite profile was established leading to a five subsite model for OPA. The pKa values of catalytic residues were determined as 5.75 and 8.36. Inhibition of OPA by monosaccharides, β-cyclodextrin and a wheat α-amylase inhibitor was studied.
KW - Ostrich Pancreas α-Amylase N-terminal sequence Subsite profile
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U2 - 10.1016/0020-711X(94)90101-5
DO - 10.1016/0020-711X(94)90101-5
M3 - Article
AN - SCOPUS:0028172849
VL - 26
SP - 1313
EP - 1321
JO - International Journal of Biochemistry and Cell Biology
JF - International Journal of Biochemistry and Cell Biology
SN - 1357-2725
IS - 10-11
ER -