| Inhibition properties of Sepharose-bound trypsin and a protease on the surface of Ehrlich ascites tumour cells. | |
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MedLine Citation:
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PMID: 6269636 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Ehrlich ascites cells have been shown to possess a protease with beta-naphthylamidase activity located on the surface of these cells. This enzyme is protected from the inhibitory action of protein inhibitors of trypsin (EC 3.4.21.4) in free solution, but is inhibited by high concentrations of active site-directed inhibitors of trypsin. We believe the protection against inhibition is provided by the location of this protease on the cell surface. We employed a model system of trypsin coupled to Sepharose to demonstrate the protective action of an inert surface, resulting in a marked reduction in inhibition of trypsin-Sepharose, compared to trypsin in free solution, when exposed to both high and low molecular weight inhibitors. This cell protease has been shown to play a role in activation of the zymogen of collagenase exported by tumour cells. This role may have important implications for tumour cell invasion of the intercellular matrix. |
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Authors:
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F S Steven; M M Griffin; G S Itzhaki; A Al-Habib |
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Publication Detail:
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Type: Comparative Study; Journal Article |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 660 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 1981 Aug |
Date Detail:
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Created Date: 1981-12-15 Completed Date: 1981-12-15 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 333-40 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Aminopeptidases
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metabolism Animals Binding Sites / drug effects Carcinoma, Ehrlich Tumor / enzymology* Cell Membrane / enzymology Enzymes, Immobilized / antagonists & inhibitors Mice Microbial Collagenase / metabolism Peptide Hydrolases / metabolism* Polysaccharides* Sepharose* Trypsin / metabolism* Trypsin Inhibitors / pharmacology* |
| Chemical | |
Reg. No./Substance:
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0/Enzymes, Immobilized; 0/Polysaccharides; 0/Trypsin Inhibitors; 9012-36-6/Sepharose; EC 3.4.-/Peptide Hydrolases; EC 3.4.11.-/Aminopeptidases; EC 3.4.21.4/Trypsin; EC 3.4.24.3/Microbial Collagenase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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