A comparison of the substrate specificities of cathepsin D and pseudorenin.
Cathepsin D, purified from hog spleen, releases angiotensin I from tetradecapeptide renin substrate and from protein renin substrates purified from hog and human plasma. However, the enzyme does not act on the naturally occurring renin substrate as it exists in plasma nor on purified substrate in the presence of plasma. Cathepsin D releases angiotensin I quantitatively from tetradecapeptide renin substrate and does not further degrade the angiotensin I on prolonged incubation. The pH optimum for cathepsin D prolonged incubation. The pH optimum for cathepsin D acting on tetradecapeptide renin substrate is 4.5, and there is very low activity above pH 7. These properties are very similar to those of pseudorenin, an angiotensin-forming enzyme originally isolated from human kidney, indicating that cathepsin D and pseudorenin may be identical.[1]References
- A comparison of the substrate specificities of cathepsin D and pseudorenin. Dorer, F.E., Lentz, K.E., Kahn, J.R., Levine, M., Skeggs, L.T. J. Biol. Chem. (1978) [Pubmed]
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