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
N1 - Funding Information:
A(.k1z0)(‘/(,Ll~(‘nl(,)ll.~-Thaeu thors gratefully acknowledge the financial support granted by the South African Foundation for Research Development and the University of Port Elizabeth, and would also like to expresst heir gratitude to the Klein Karoo Agricultural Co-operative at Oudt- shoorn, South Africa, for the experimental material. The authors would also like to express their gratitude to Professors P. R. Hall and J. W. Consalves of the Department of Mathematics and Applied Mathematics, University of Port Elizabeth, South Africa, for assistancei n calculation of subsite affinities for OPA.
PY - 1994
Y1 - 1994
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
UR - http://www.scopus.com/inward/record.url?scp=0028172849&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028172849&partnerID=8YFLogxK
U2 - 10.1016/0020-711X(94)90101-5
DO - 10.1016/0020-711X(94)90101-5
M3 - Article
AN - SCOPUS:0028172849
SN - 1357-2725
VL - 26
SP - 1313
EP - 1321
JO - International Journal of Biochemistry
JF - International Journal of Biochemistry
IS - 10-11
ER -