| L-usnate-urease interactions: binding sites for polymerization. | |
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MedLine Citation:
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PMID: 6223456 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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L-usnic acid inactivates urease through a process which implicates the blockade of--SH groups in parallel to the formation of inactive polymers. Both L-alanine and L-proline partially reverses the inactivation and effectively diminishes the amount of highly polymerized protein. The amino acids also prevent the linkage of L-usnic acid on the sites of low affinity for the ligand, being then related to the sites of polymerization. |
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Authors:
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B Cifuentes; I García; C Vicente |
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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: Zeitschrift für Naturforschung. Section C: Biosciences Volume: 38 ISSN: 0341-0382 ISO Abbreviation: Z. Naturforsch., C, Biosci. Publication Date: 1983 Mar-Apr |
Date Detail:
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Created Date: 1983-08-11 Completed Date: 1983-08-11 Revised Date: 2009-06-08 |
Medline Journal Info:
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Nlm Unique ID: 7801143 Medline TA: Z Naturforsch C Country: GERMANY, WEST |
Other Details:
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Languages: eng Pagination: 273-6 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Alanine
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pharmacology Benzofurans* Kinetics Proline / pharmacology Protein Binding Urease / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Benzofurans; 147-85-3/Proline; 56-41-7/Alanine; EC 3.5.1.5/Urease |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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