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  • Buttle, David J (author)

Interactions of papaya proteinase IV with inhibitors

  • Article/chapterEnglish1990

Publisher, publication year, extent ...

  • 1990

Numbers

  • LIBRIS-ID:oai:lup.lub.lu.se:fccddff6-4b6c-4793-9724-92b0d18c8e88
  • https://lup.lub.lu.se/record/1105562URI
  • https://doi.org/10.1016/0014-5793(90)80153-ADOI

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  • Language:English
  • Summary in:English

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  • Subject category:art swepub-publicationtype
  • Subject category:ref swepub-contenttype

Notes

  • Papaya proteinase IV (PPIV) is not inhibited by chicken cystatin, or human cystatins A or C, unlike most other proteinases of the papain superfamily. The enzyme inactivates chicken cystatin and human cystatin C by limited proteolysis of the glycyl bond previously shown to be involved in the inhibitory inactivity of the cystatins, but has no action on cystatin A. Contamination of commercial crystalline papain with PPIV accounts for the limited proteolysis of cystatins by ‘papain’ reported previously. PPIV is slowly bound by human α2-macroglobulin. The enzyme is irreversibly inactivated by E-64, and by peptidyl diazomethanes containing glycine in P1 and a hydrophobic side-chain in P2. The reaction of PPIV with iodoacetate is extremely slow. PPIV is inhibited by peptide aldehydes despite the presence of bulky sidechains in P1, suggesting that these reversible inhibitors do not bind as substrate analogues.

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Added entries (persons, corporate bodies, meetings, titles ...)

  • Ritonja, Anka (author)
  • Dando, Pamela M (author)
  • Abrahamson, MagnusLund University,Lunds universitet,Avdelningen för klinisk kemi och farmakologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Clinical Chemistry and Pharmacology,Department of Laboratory Medicine,Faculty of Medicine(Swepub:lu)kkem-mab (author)
  • Shaw, Elliot N (author)
  • Wikstrom, Peter (author)
  • Turk, Vito (author)
  • Barrett, Alan J (author)
  • Avdelningen för klinisk kemi och farmakologiInstitutionen för laboratoriemedicin (creator_code:org_t)

Related titles

  • In:FEBS Letters262:1, s. 58-601873-3468

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