Collect. Czech. Chem. Commun.
1979, 44, 288-293
https://doi.org/10.1135/cccc19790288
Hog pancreatic α-amylase. Preparation and characterization
Ivan Kluh
Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, 166 10 Prague 6
Abstract
Crystalline α-amylase (EC 3.2.1.1) was prepared from hog pancreas. The preparation obtained was resolved into two isozymes by chromatography on DEAE-cellulose. The molecular weight (51 500), amino acid composition, and terminal groups of both isozymes were determined. Both isozymes have a single polypeptide chain containing 460-465 amino acid residues. The amino acid composition of both isozymes is similar. None of them has a free N-terminal end group. Both isozymes are C-terminated with leucine. The molecule of each isozyme is cross-linked by 5 disulfide bonds and contains two sulfhydryl groups.
