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 language | English (US) |
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Pages (from-to) | 2237-2240 |
Number of pages | 4 |
Journal | Biochemical Pharmacology |
Volume | 26 |
Issue number | 23 |
DOIs | |
State | Published - Dec 1 1977 |