These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Study of the immobilization of alcohol dehydrogenase on Au-colloid modified gold electrode by piezoelectric quartz crystal sensor, cyclic voltammetry, and electrochemical impedance techniques.
    Author: Liu Y, Yin F, Long Y, Zhang Z, Yao S.
    Journal: J Colloid Interface Sci; 2003 Feb 01; 258(1):75-81. PubMed ID: 12600773.
    Abstract:
    The immobilization of alcohol dehydrogenase (ADH) on Au-colloid modified gold electrodes has been investigated. Colloidal Au was first self-assembled onto gold electrodes through the thiol groups of an 1,6-hexanedithiol monolayer. Piezoelectric quartz crystal sensor, cyclic voltammetry, and electrochemical impedance techniques were used to investigate the immobilization of ADH on Au colloids. The cyclic voltammogram tends to be more irreversible with increased ADH concentration. In the impedance spectroscopic study, an obvious difference of the electron transfer resistance between the Au-colloid modified electrode and the bare gold electrode was observed. Using the piezoelectric quartz crystal sensor, the Michaelis constant, K(m), and the maximum initial rate, V(max), of the immobilized ADH were estimated as 6.03 x 10(-4) M and 0.63 Hzs (-1), respectively. The binding constant of ADH with nicotinamide adenine dinucleotide (NAD) was also determined as 1.87 x 10(4) M(-1). Experimental results showed that colloidal Au can be used as a biocompatible matrix for enzyme immobilization.
    [Abstract] [Full Text] [Related] [New Search]