Purification of porcine enterokinase by affinity chromatography
- 1 May 1975
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 147 (2) , 363-366
- https://doi.org/10.1042/bj1470363
Abstract
A method is described for the purification of porcine enterokinase by affinity chromatography with p-aminobenzamidine as the ligand. Purification was completed by immunoadsorption with antisera raised to components binding non-biologically to the gel. The final enterokinase preparation was 2.3 times more active than the most active preparation previously described.Keywords
This publication has 13 references indexed in Scilit:
- Effect of ionic strength and calcium ions on the activation of trypsinogen by enterokinase: A modified test for the quantitative evaluation of this enzymeBiochimica et Biophysica Acta (BBA) - Enzymology, 1973
- On porcine enterokinase. Further purification and some molecular propertiesBiochimica et Biophysica Acta (BBA) - Enzymology, 1973
- Affinity chromatograpy: Purification of bovine trypsin and thrombinArchives of Biochemistry and Biophysics, 1973
- Single Step Purification of Ovine Luteinizing Hormone by Affinity ChromatographyJournal of Biological Chemistry, 1972
- Purification and Specificity of Porcine EnterokinaseJournal of Biological Chemistry, 1971
- Studies on intestinal disaccharidases. V. Characterization and properties of maltase fractions from monkey intestine.1970
- Inhibitory effect of aromatic diamidines on trypsin and enterokinaseCellular and Molecular Life Sciences, 1969
- Assay of intestinal disaccharidasesAnalytical Biochemistry, 1968
- A spectrophotometric determination of trypsin and chymotrypsinBiochimica et Biophysica Acta, 1955
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951