Lysyl oxidase (LOX) is a copper-containing enzyme necessary for the structural integrity and stability of matrix proteins such as collagen and elastin. Published procedures for the isolation of LOX results in wide range of enzyme purity and activity; ultimately believed to be a contributing factor behind the still unanswered question regarding the role of copper in the catalytic mechanism of LOX. Due to LOX's intrinsically low solubility in aqueous buffers, new approaches were attempted in an effort to selectively solubilize and isolate the enzyme from other co-eluted impurities routinely observed during purification. Biodetergents are commonly used to purify, isolate or solubilize membrane proteins while preserving the protein's biological activity. Therefore, incorporation of several biodetergents varying in their ionic strengths and concentrations into the extractions during the initial stages of the purification, their effects on increasing the solubility of the co-purified matrix proteins and the enzyme itself will be presented.

Application of biodetergents for the facilitation of the lysyl oxidase purification

245th National Meeting (2013)

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