Collect. Czech. Chem. Commun.
1984, 49, 1846-1853
https://doi.org/10.1135/cccc19841846
Post-proline endopeptidase, further characterization of the enzyme from pig kidneys
Karel Hauzer, Tomislav Barth, Linda Servítová and Karel Jošt
Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, 166 10 Prague 6
Abstract
A post-proline endopeptidase (EC 3.4.21.26) was isolated from pig kidneys using a modified method described earlier. The enzyme was further purified by ion exchange chromatography on DEAE-Sephacel. The final product contained about 95% of post-proline endopeptidase. The enzyme molecule consisted of one peptide chain with a relative molecular mass of 65 600 to 70 000, containing a large proportion of acidic and alifatic amino acids (glutamic acid, aspartic acid and leucine) and the N-terminus was formed by aspartic acid or asparagine. In order to prevent losses of enzyme activity, thiol compounds has to be added.
