Aspartic proteinases: their activation and structural studies.

V Turk; V Puizdar; T Lah; I Kregar

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PubMed · 6762543

Aspartic proteinases: their activation and structural studies.

V Turk·V Puizdar·T Lah·I Kregar

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Abstract

Besides extracellular mammalian aspartic proteinases also intracellular proteinase cathepsin D is synthesized in the form of a precursor. The evidence is presented that cathepsin D zymogen (cathepsinogen D, procathepsin D) can be activated by a similar mechanism to that of pepsin, releasing an activation segment - peptide(s). The released peptide(s) show inhibitory activity towards cathepsin D and some other aspartic proteinases. The activation peptides released from bovine pepsinogen do not inhibit cathepsins D and E. The structure of different aspartic proteinases was studied by circular dichroism measurements. The binding of pepstatin causes conformational changes in the near UV CD spectrum.

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Amino Acids Aspartic Acid Endopeptidases Cathepsin D Cathepsins Circular Dichroism Endopeptidases Enzyme Activation Enzyme Precursors Hydrogen-Ion Concentration Protein Conformation Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

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V Turk, V Puizdar, T Lah, I Kregar. 1982. Aspartic proteinases: their activation and structural studies.. https://pubmed.ncbi.nlm.nih.gov/6762543/

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