Vaughan Oosthuizen, Ryno J. Naudé, Willem Oelofsen
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Ostrich α-amylase: Purification and characterization of the pancreatic isoenzymes
1.
1. Four ostrich pancreatic α-amylase isoenzymes were isolated by isoelectric focusing, following affinity chromatography on cyclohepta-amylose-Sepharose 4B.
2.
2. Amino acid compositions of the four isoenzymes are very similar with only one charged amino acid (Arg) being significantly different.
3.
3. The molecular weights, as determined by SDS-PAGE and amino acid composition, are nearly identical (52–53 kDa) for all four isoenzymes.
4.
4. The four α-amylase isoenzymes appear to be kinetically distinct enzymes with a requirement for calcium.
5.
5. Ostrich α-amylase isoenzymes appear to be non-glycosylated and contain one free thiol group.
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