Two-step affinity-chromatographic purification of cathepsin D from pig myometrium with high yield
- 31 July 1981
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 197 (2), 519-522
- https://doi.org/10.1042/bj1970519
Abstract
Cathepsin D was purified by 2-step affinity chromatography on concanavalin A- and pepstatin-Sepharose. The main purification was achieved by washing the enzyme bound to the pepstatin-Sepharose column with buffered 6 M-urea. This step separated cathepsin D from all low and high MW impurities. Although the 1700-fold purified acid proteinase was homogeneous on sodium dodecyl sulfate/polyacrylamide-gel electrophoresis, it still showed microheterogeneity.This publication has 11 references indexed in Scilit:
- Early events in the biosynthesis of the lysosomal enzyme cathepsin D.Journal of Biological Chemistry, 1979
- Cathepsin D isozymes from porcine spleens. Large scale purification and polypeptide chain arrangements.Journal of Biological Chemistry, 1979
- Proteinase and proteinase-inhibitor activities of rat uterine myometrium during pregnancy and involutionBiochemical Journal, 1979
- Interaction of human cathepsin D with the inhibitor pepstatinBiochemical Journal, 1976
- INTRACELLULAR PROTEIN BREAKDOWN .6. PREPARATION, PROPERTIES AND BIOLOGICAL SIGNIFICANCE OF CATHEPSIN D FROM RAT-LIVER (EC 3.4.4.23)1976
- [9] Hydrophobic chromatographyMethods in Enzymology, 1974
- Maturation of the head of bacteriophage T4Journal of Molecular Biology, 1973
- Adsorbents for affinity chromatography. Use of N-hydroxysuccinimide esters of agaroseBiochemistry, 1972
- Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads.1970
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951