@article{citeulike:470526,
	title = {Amperometric immunosensors based on protein A coupled polyaniline-perfluorosulfonated ionomer composite electrodes.},
	address = {Department of Chemistry, National Sun Yat-sen University, Kaohsiung, Taiwan.},
	author = {C. H. Liu and K. T. Liao and H. J. Huang},
	journal = {Anal Chem},
	month = {July},
	number = {13},
	pages = {2925--2929},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=10905329},
	volume = {72},
	year = {2000},
	biburl = {http://www.bibsonomy.org/bibtex/26c03a3547c820c8605fb10f76077e1f0/biblio24},
	abstract = {A very sensitive immunosensor based on polyaniline/ Nafion/protein A (PA/NF/PrA) composite electrodes has been developed for the amperometric immunoanalysis with urease-labeled immunoreagents. The use of urease conjugated goat anti-RIgG (GaRIgG-Ur) as the labeled antibody and urea as the substrate with an amperometric detection at -200 mV (vs Ag/AgCl) resulted in a dynamic range of 50-2000 ng mL-1 and a low detection limit of 10 ng/mL (64 pM) for the immunoanalysis of rabbit immunoglobulin G (RIgG). Because of the special affinity between protein A and RIgG, the PA/NF/PrA electrode can be regenerated repetitively by changing the pH of the buffer solutions. Characteristics of the PA/NF/PrA/RIgG immunosensor and optimal conditions for the competitive immunoanalysis of RIgG with FIA were studied.},
	issn = {0003-2700}, doi = {10.1021/ac9914317}, citeulike-article-id = {470526}, priority = {2},
	keywords = {ag_detection amperometry electrochemistry immunoassay immunoelectrode immunosensor sandwich }
}

@article{citeulike:471085,
	title = {Immunosensing with amperometric detection, using galactosidase as label and  as substrate},
	author = {Mar Massen and Zheng Liu and Tetsuya Haruyama and Eiry Kobatake and Yoshihito Ikariyama and Masuo Aizawa},
	journal = {Analytica Chimica Acta},
	month = {April},
	number = {3},
	pages = {353--359},
	url = {http://www.sciencedirect.com/science/article/B6TF4-3YKKPWK-8W/2/6c0722c5716397552432184c88c21f84},
	volume = {304},
	year = {1995},
	biburl = {http://www.bibsonomy.org/bibtex/273c5e495d6d00a1775312d6af9d71a79/biblio24},
	abstract = {(PAPG) was shown to be a suitable substrate for the amperometric detection of galactosidase activity at neutral pH. The application of this amplification system for immunoassay was demonstrated. The product of the enzyme reaction, p-aminophenol (PAP), was detected at 200 mV, vs. Ag/AgCl, by flow-injection analysis (FIA), with a 50 nM detection limit. PAPG was hydrolyzed more than 2.5 times faster than , by the enzyme. Both PAP and PAPG were stable at pH 7. The galactosidase concentration could be measured down to a concentration of 100 fM, and mouse IgG could be assayed by sandwich immunoassay down to 700 fM. PAPG was found to be a promising reagent for heterogeneous systems, like the one described, and for homogenous assays of biological fluids.},
	doi = {10.1016/0003-2670(94)00645-3}, citeulike-article-id = {471085}, priority = {2},
	keywords = {ag_detection amperometry fia heterogeneous immunoassay }
}