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

Rodney L. Johnson; Alan M. Poisner

doi:10.1016/0006-2952(77)90285-4

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

Rodney L. Johnson, Alan M. Poisner

Medicinal Chemistry

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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)
Pages (from-to)	2237-2240
Number of pages	4
Journal	Biochemical Pharmacology
Volume	26
Issue number	23
DOIs	https://doi.org/10.1016/0006-2952(77)90285-4
State	Published - Dec 1 1977

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title = "Evidence that pseudorenin activity in bovine spleen is due to cathepsin D",

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.",

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T1 - Evidence that pseudorenin activity in bovine spleen is due to cathepsin D

AU - Johnson, Rodney L.

AU - Poisner, Alan M.

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N2 - 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.

AB - 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.

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

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