Purification of enzymatically active recombinant lysyl oxidase and lysyl oxidase-like 2 proteins from mammalian cells
Tash, Esraa Abdulgader
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Lysyl oxidase is a copper-dependent enzyme responsible for the development of lysine-derived cross-links in structural extracellular matrix proteins. Recent reports have revealed that LOX and possibly LOXL proteins exhibit biological effects and tissue distributions suggesting that these proteins play exceptionally important roles in biology beyond the induction of cross-linkage formation in collagen and elastin. Several new functions, as varied as tumor suppression, cellular sequence, developmental control, and chemotaxis have been assigned to LOX. The importance of LOX has been further emphasized by the findings that abnormal LOX activity contributes to a number of different diseases, including atherosclerosis, aortic aneurysms, pulmonary fibrosis, and hepatic fibrosis. Subsequent studies on the specific functions of each LOX family member is necessary to understand the mechanics of the different functions of these proteins, which will be heipfull in developing therapeutic treatments for the diseases associated with abnormal levels of LOX. The aim of this study is to purify large yields of active forms of recombinant LOX and LOXL2 from mammalian cells. It was found that the enzyme activity of the recombinant LOXL2 expressed by the purified LOXL2 celIs was 7.1 fold that of its control celIs after loading equal protein when measuring the enzyme activity which was calculated from the BCA assay prior to the amplex red assay. Expression and purification of LOXL2 in considerable amount was confirmed by Western blot. This expression and purification will aid in revealing the exact structure of LOX and its family, which will give an idea about the structure-function relationship of this protein.
PLEASE NOTE: This work is protected by copyright. Downloading is restricted to the BU community: please click Download and log in with a valid BU account to access. If you are the author of this work and would like to make it publicly available, please contact firstname.lastname@example.org.Thesis (MSD) --Boston University, Henry M. Goldman School of Dental Medicine, 2015 (Department of Periodontology).Includes bibliography: leaves 35-36.
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