| Identification of the disulfide bonds of lysyl oxidase. | |
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MedLine Citation:
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PMID: 21188434 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Proteolytic digestion of bovine aortic lysyl oxidase followed by tandem mass spectrometry has enabled assignment of all five disulfide bonds. The results indicate that the enzyme has a very stable central core containing three disulfide bonds, the lysyl tyrosyl quinone cross-link and the copper. This core is well isolated from solvent with the result that the oxidized (normal) form of the enzyme is remarkably resistant to proteolysis and is unusually stable at high temperatures and in the presence of denaturants. |
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Authors:
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Xi Chen; Frederick T Greenaway |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2010-12-28 |
Journal Detail:
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Title: Journal of neural transmission (Vienna, Austria : 1996) Volume: - ISSN: 1435-1463 ISO Abbreviation: - Publication Date: 2010 Dec |
Date Detail:
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Created Date: 2010-12-28 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9702341 Medline TA: J Neural Transm Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Carlson School of Chemistry and Biochemistry, Clark University, 950 Main St, Worcester, MA, 01610-1477, USA. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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