Document Detail

Identification of the disulfide bonds of lysyl oxidase.
MedLine Citation:
PMID:  21188434     Owner:  NLM     Status:  Publisher    
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.
Xi Chen; Frederick T Greenaway
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2010-12-28
Journal Detail:
Title:  Journal of neural transmission (Vienna, Austria : 1996)     Volume:  -     ISSN:  1435-1463     ISO Abbreviation:  -     Publication Date:  2010 Dec 
Date Detail:
Created Date:  2010-12-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9702341     Medline TA:  J Neural Transm     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Carlson School of Chemistry and Biochemistry, Clark University, 950 Main St, Worcester, MA, 01610-1477, USA.
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