| Interaction between squash inhibitors and bovine trypsinogen. | |
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MedLine Citation:
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PMID: 2059335 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Squash seeds proteinase inhibitors form stoichiometric complexes with bovine trypsinogen. In terms of association constants (Ka), the interaction is weak. The inhibitors bind to the zymogen with Ka values of approx. 10(4)M-1 i.e. 2 X 10(7) times weaker than to bovine beta-trypsin. Squash inhibitor with Lys at the P1 position binds to trypsinogen with a Ka value 2.1-fold higher than the inhibitor with Arg at P1. The Ile-Val binding cleft and the Ca2+ binding site of trypsinogen are cooperatively linked to the inhibitor binding site. Although these three sites are spatially separated, either binding of calcium ion or Ile-Val dipeptide to trypsinogen increase the Ka values 3-fold and more than 100-fold, respectively. In the presence of Ile-Val trypsinogen resynthetizes extremely slowly (about 10(4) times slower than beta-trypsin) the reactive site peptide bond in squash inhibitors. |
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Authors:
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T Zbyryt; J Otlewski |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biological chemistry Hoppe-Seyler Volume: 372 ISSN: 0177-3593 ISO Abbreviation: Biol. Chem. Hoppe-Seyler Publication Date: 1991 Apr |
Date Detail:
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Created Date: 1991-08-08 Completed Date: 1991-08-08 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 8503054 Medline TA: Biol Chem Hoppe Seyler Country: GERMANY |
Other Details:
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Languages: eng Pagination: 255-62 Citation Subset: IM |
Affiliation:
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Institute of Biochemistry, University of Wroclaw, Poland. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Binding Sites Calcium / metabolism Cattle Dipeptides / metabolism Hydrogen-Ion Concentration Kinetics Molecular Sequence Data Ovomucin Plant Proteins / metabolism* Trypsin / metabolism* Trypsin Inhibitors / metabolism* Trypsinogen / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Dipeptides; 0/Plant Proteins; 0/Trypsin Inhibitors; 0/trypsin inhibitor, Cucurbita sp.; 37281-36-0/Ovomucin; 41017-96-3/isoleucylvaline; 7440-70-2/Calcium; 9002-08-8/Trypsinogen; EC 3.4.21.4/Trypsin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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