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Interactions of pap...
Interactions of papaya proteinase IV with inhibitors
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Buttle, David J (author)
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Ritonja, Anka (author)
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Dando, Pamela M (author)
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- Abrahamson, Magnus (author)
- Lund 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
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Shaw, Elliot N (author)
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Wikstrom, Peter (author)
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Turk, Vito (author)
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Barrett, Alan J (author)
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(creator_code:org_t)
- 1990
- 1990
- English.
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In: FEBS Letters. - 1873-3468. ; 262:1, s. 58-60
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http://dx.doi.org/10...
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- Macroglobulin
- α2-
- Cystatin
- Compound E-64
- Iodoacetate
- Iodoacetamide
- Papain
- Peptide aldehyde
- Peptidyl diazomethane
Publication and Content Type
- art (subject category)
- ref (subject category)
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