Chemistry

Identification of the disulfide bonds of lysyl oxidase

Document Type

Conference Proceeding

Abstract

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. © Springer-Verlag 2010.

Publication Title

Journal of Neural Transmission

Publication Date

7-2011

Volume

118

Issue

7

First Page

1111

Last Page

1114

ISSN

0300-9564

DOI

10.1007/s00702-010-0560-y

Keywords

cysteine content, disulfide linkages, lysyl oxidase, tandem mass spectrometry

Cross Post Location

Student Publications

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