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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Glycerol-induced development of catalytically active conformation of Crotalus adamanteus L-amino acid oxidase in vitro.

The reconstitutable apoprotein of Crotalus adamanteus L-amino acid oxidase was prepared using hydrophobic interaction chromatography. After reconstitution with flavin adenine dinucleotide, the resulting protein was inactive, with a perturbed conformation of the flavin binding site. Subsequently, a series of cosolvent-dependent compact intermediates was identified. The nearly complete activation of the reconstituted apoprotein and the restoration of its native flavin binding site was achieved in the presence of 50% glycerol. We provide evidence that in addition to a merely stabilizing effect of glycerol on native proteins, glycerol can also have a restorative effect on their compact equilibrium intermediates, and we suggest the hydrophobic effect as a dominating force in this in vitro-assisted restorative process.[1]

References

  1. Glycerol-induced development of catalytically active conformation of Crotalus adamanteus L-amino acid oxidase in vitro. Raibekas, A.A., Massey, V. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
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