Evidence that pseudorenin activity in bovine spleen is due to cathepsin D

Rodney L. Johnson, Alan M. Poisner

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

Pseudorenin and cathepsin D activity from bovine spleen were found to behave identically on DEAE-cellulose, Sephadex G-100, and concanavalin A-agarose chromatography. The molecular weight of pseudorenin and of cathepsin D was estimated to be 50,000. The binding of the enzymatic activity to concanavalin A-agarose and elution with α-methyl-d-mannoside indicates that pseudorenin (cathepsin D) is a glycoprotein. It is suggested that pseudorenin activity in the spleen is due to cathepsin D.

Original languageEnglish (US)
Pages (from-to)2237-2240
Number of pages4
JournalBiochemical Pharmacology
Volume26
Issue number23
DOIs
StatePublished - Dec 1 1977

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