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Action of cathepsin D on fructose-1,6-bisphosphate aldolase.

Cathepsin D inactivated aldolase at pH values between 4.2 and 5.2; the chloride, sulphate or iodide, but not citrate or acetate, salts of sodium or potassium accelerated the rate of inactivation. Cathepsin D cleaved numerous peptide bonds in the C-terminus of aldolase, but the major site of cleavage...

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Bibliographic Details
Main Authors: Offermann, M K, Chlebowski, J F, Bond, J S
Format: Artigo
Language:Inglês
Published: 1983
Subjects:
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC1154396/
https://ncbi.nlm.nih.gov/pubmed/6882356
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