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Afting, E.G. et al.

Two-step affinity-chromatographic purification of cathepsin D from pig myometrium with high yield.

Cathepsin D was purified by two-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-molecular-weight impurities. Although the 1700-fold purified acid proteinase was homogeneous on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, it still showed microheterogeneity.[1]

References

Two-step affinity-chromatographic purification of cathepsin D from pig myometrium with high yield. Afting, E.G., Recker, M.L. Biochem. J. (1981) [Pubmed]

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