The existence of a precursor of cathepsin D: evidence from autolysis, denaturation and activation studies.
This report evidences that the single polypeptide chain of cathepsin D undergoes in vitro autolysis resulting in heavy (Mr about 30000) and light (Mr about 15000) polypeptide chains. These two chains are held together through non-covalent interaction, thus constituting a stable active conformation. Fluorescence and circular dichroism measurements demonstrate the irreversible denaturation of cathepsin D. The existence of cathepsin D precursor, cathepsinogen D, of about 50000 molecular weight was proved. Cathepsinogen D is converted to the active enzyme by intramolecular activation, releasing activation-inhibitory peptide(s).
D000818:Animals; D002402:Cathepsin D; D002403:Cathepsins / Q000302:isolation & purification / Q000378:metabolism*; D002417:Cattle; D002942:Circular Dichroism; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D011487:Protein Conformation; D011489:Protein Denaturation
D004792:Enzyme Precursors; D002403:Cathepsins; D002402:Cathepsin D