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Enzyme Activity of α-chymotrypsin: Deactivation by Gold Nano-Cluster and Reactivation by Glutathione

Enzyme Activity of α-chymotrypsin: Deactivation by Gold Nano-Cluster and Reactivation by Glutathione

Catherine Ghosh, Tridib Mondal, Kankan Bhattacharyya

J Colloid Interface Sci. 2017 May 15;494:74-81.

PMID: 28135630

Abstract:

Effect of gold nanoclusters (Au-NCs) on the circular dichroism (CD) spectra and enzymatic activity of α-chymotrypsin (ChT) (towards hydrolysis of a substrate, N-succinyl-l-phenylalanine p-nitroanilide) are studied. The CD spectra indicate that on binding to Au-NC, ChT is completely unfolded, resulting in nearly zero ellipticity. α-chymotrypsin (ChT) coated gold nano-clusters exhibit almost no enzymatic activity. Addition of glutathione (GSH) or oxidized glutathione (GSSG) restore the enzyme activity of α-chymotrypsin by 30-45%. ChT coated Au-NC exhibits two emission maxima-one at 480nm (corresponding to Au10) and one at 640nm (Au25). On addition of glutathione (GSH) or oxidized glutathione (GSSG) the emission peak at 640nm vanishes and only one peak at 480nm (Au10) remains. MALDI mass spectrometry studies suggest addition of glutathione (GSH) to α-chymotrypsin capped Au-NCs results in the formation of glutathione-capped Au-NCs and α-chymotrypsin is released from Au-NCs. CD spectroscopy indicates that the conformation of the released α-chymotrypsin is different from that of the native α-chymotrypsin.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9004073-A	Chymotrypsin		9004-07-3	Price

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