@article{citeulike:477551,
        title = {An amperometric enzyme-channeling immunosensor.},
        address = {Department of Molecular Microbiology \& Biotechnology, Tel-Aviv University, Israel. Rishpon@post.TAU.AC.IL},
        author = {J. Rishpon and D. Ivnitski},
        journal = {Biosens Bioelectron},
        number = 3,
        pages = {195--204},
        volume = 12,
        year = 1997,
        url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=9115687},
        id = {477551},
	issn = {0956-5663},
	priority = {2},
	comment = {Rishpon@post.TAU.AC.IL/requested},
	abstract = {This paper presents a new disposable amperometric, enzyme-channeling immunosensor for a quantitative, rapid, separation-free enzyme immunoassay (EIA) that can be used in clinical diagnostics, as well as in biomedical, biochemical, and environmental research. The sensor consists of a disposable, polymer-modified, carbon electrode on which enzyme 1 is coimmobilized with a specific antibody that binds the corresponding antigen in a test solution. The solution also contains a conjugate of enzyme 2. An immunological reaction brings the two enzymes into close proximity at the electrode surface, and the signal is amplified through enzyme channeling. The localization of both enzymes on the electrode surface limits the enzymatic reactions to the polymer/membrane/electrode interface. The sensor overcomes the problem of discriminating between the signal that is produced by the immuno-bound enzyme label on the electrode surface and the background level of signal that emerges from the bulk solution. Combining enzyme-channeling reactions, optimizing hydrodynamic conditions, and electrochemically regenerating mediators within the membrane layer of the antibody electrode significantly increased the signal-to-noise ratio of the sensor. The amperometric enzyme-channeling immunosensor enabled the performance of separation-free EIAs without washing steps, resulting in a relatively short assay time of 5-30 min for the complete immunoassay, compared with at least 1-3 h for ELISA methods. Model systems using peroxidase-antibody, biotin-avidin, viral antigens (CD4-gp120), and bacteria (Staphylococcus aureus) were investigated. S. aureus cells were detected in pure culture at concentrations as low as 1000 cells/ml.},
	biburl = {http://www.bibsonomy.org/bibtex/2da5c7c667c7d74efe67fd77b37abcca4/biblio24},
	keywords = {immunoassay homogeneous electrochemistry immunosensor ecia ag_detection amperometry}
}

@article{citeulike:485887,
        title = {Enzyme channeling immunoassay: A new homogeneous enzyme immunoassay technique},
        author = {David J. Litman and Teresa M. Hanlon and Edwin F. Ullman},
        journal = {Analytical Biochemistry},
        month = {July},
        number = 1,
        pages = {223--229},
        volume = 106,
        year = 1980,
        url = {http://www.sciencedirect.com/science/article/B6W9V-4DYM9HN-GJ/2/a00c4ded6bf14b3df23e1f40ab0fa2a4},
        id = {485887},
	priority = {2},
	doi = {10.1016/0003-2697(80)90141-4},
	abstract = {A homogeneous enzyme immunoassay has been developed in which an antigen and glucose-6-phosphate dehydrogenase are coimmobilized on agarose beads. Binding of hexokinase-labeled antibody to the bead-bound antigen results in an accelerated conversion of glucose, ATP, and NAD+ to 6-phosphogluconolactone, ADP, and NADH. Critical parameters affecting assay response are discussed.},
	biburl = {http://www.bibsonomy.org/bibtex/240d83bdeaf486fa65eaee25d645f54fd/biblio24},
	keywords = {immunoassay homogeneous ecia ag_detection}
}

@article{citeulike:485944,
        title = {Ultrasound-accelerated immunoassay, as exemplified by enzyme immunoassay of choriogonadotropin.},
        author = {R. Chen and L. Weng and N. C. Sizto and B. Osorio and C. J. Hsu and R. Rodgers and D. J. Litman},
        journal = {Clin Chem},
        month = {September},
        number = 9,
        pages = {1446--1451},
        volume = 30,
        year = 1984,
        url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=6380810},
        id = {485944},
	issn = {0009-9147},
	priority = {2},
	abstract = {The rate-limiting step in many solid-phase immunoassays is associated with the slow kinetics of binding of macro-molecular antigen and conjugate to the immobilized phase. We demonstrate that the use of ultrasonic energy to enhance mass transport across liquid/solid interfaces can dramatically accelerate antigen binding to immobilized antibodies. We use an ultrasound-accelerated procedure with an enzyme-channelling test strip containing glucose oxidase and specific antibody to the alpha-subunit of human choriogonadotropin (HCG) co-immobilized onto a cellulose support. A horseradish peroxidase conjugate of monospecific antibody to the beta-subunit of HCG is used in the liquid phase to complete the immune "sandwich." Use of ultrasound to accelerate binding and of enzyme channelling to eliminate wash steps result in a simple two-incubation protocol by which 25 int. units of urinary HCG per liter can be detected visually in less than 20 min of assay time.},
	biburl = {http://www.bibsonomy.org/bibtex/264c40cb08d352ce7e4ac71f237f96e39/biblio24},
	keywords = {immunoassay ecia ag_detection}
}

@article{citeulike:485945,
        title = {Bioluminescent immunosorbent for rapid immunoassays.},
        author = {B. Térouanne and M. L. Carrié and J. C. Nicolas and A. Crastes de Paulet},
        journal = {Anal Biochem},
        month = {April},
        number = 1,
        pages = {118--125},
        volume = 154,
        year = 1986,
        url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=3518535},
        id = {485945},
	issn = {0003-2697},
	priority = {2},
	abstract = {We describe a bioluminescent immunoassay procedure which does not require a separation step to remove excess free label. A luminescent immunosorbent constituted of bacterial luciferase, FMN oxidoreductase, and an antibody coimmobilized on Sepharose is used to determine specifically the label enzyme (glucose-6-phosphate dehydrogenase, coupled to an antigen) bound by a specific antibody. The immunosorbent confines the bioluminescent reaction in a small volume, and the bound label produces NADH, which is directly used by the nearby luciferase FMN oxidoreductase enzyme system. On the contrary NADH produced by dehydrogenases in solution is directly oxidized without emitting light. Dehydrogenases contained in the biological sample do not interfere with the assay, which can be performed directly on 25 microliter of serum. In this paper we describe the general procedure and we analyze the different parameters that must be optimized.},
	biburl = {http://www.bibsonomy.org/bibtex/2b2c1cb344c41b41bfe4f69c0aafe9a35/biblio24},
	keywords = {immunoassay ecia ag_detection}
}

@article{citeulike:485948,
        title = {Potentiometric enzyme channeling immunosensor for proteins.},
        address = {Department of Chemistry, University of Michigan, Ann Arbor 48109-1055.},
        author = {D. V. Brown and M. E. Meyerhoff},
        journal = {Biosens Bioelectron},
        number = 7,
        pages = {615--622},
        volume = 6,
        year = 1991,
        url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=1756003},
        id = {485948},
	issn = {0956-5663},
	priority = {2},
	abstract = {A potentiometric immunosensor for the detection of human IgG has been developed using an asymmetric, ion-selective membrane with immobilized adenosine deaminase and IgG. A protein A-alkaline phosphatase conjugate binds to the immobilized IgG, creating a bienzymatic catalytic layer. In the presence of sample IgG, the conjugate does not bind to the membrane. Instead, the intermediate in the two-step reaction (adenosine) must diffuse to the membrane surface, reducing the rate of product (ammonium) formation within the diffusion layer detected by the membrane. The immunosensor demonstrated is for the determination of IgG. A simplified model is described to predict the maximum rate enhancement for the 'channeled' versus 'unchanneled' reaction mechanisms.},
	biburl = {http://www.bibsonomy.org/bibtex/28affe5698f8b5e29dc5f4dc4017447ed/biblio24},
	keywords = {immunoassay potentiometry electrochemistry ecia ag_detection competition}
}

@article{citeulike:485950,
        title = {A one-step, separation-free amperometric enzyme immunosensor.},
        address = {Department of Molecular Microbiology and Biotechnology, Tel-Aviv University, Ramat-Aviv, Israel.},
        author = {D. Ivnitski and J. Rishpon},
        journal = {Biosens Bioelectron},
        number = 4,
        pages = {409--417},
        volume = 11,
        year = 1996,
        url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=8746187},
        id = {485950},
	issn = {0956-5663},
	priority = {2},
	abstract = {A new one-step, separation-free, amperometric enzyme immunosensor is described. The sensor consists of an antibody electrode that is low cost, disposable, and operates without washing or separation steps. The immunosensor combines the following signal-amplification systems: enzyme-channeling immunoassay; accumulation of the redox mediators (I2/I-); cyclic regeneration of an enzyme (peroxidase) substrate at the (polyethylenimine) polymer/electrode interface; and control of the hydrodynamic conditions at the interface of the antibody electrode. The immunological reactions were monitored electrochemically in situ, and the binding curves were directly visualized on a computer screen. The complete immunoassay can be performed in 5-20 min depending on the complexity of the immunological reactions. Model systems using rabbit IgG and human luteinizing hormone (hLH) in a 'sandwich' immunoassay revealed that the immunosensor can detect concentrations of hLH in human serum as low as 1 ng ml-1.},
	biburl = {http://www.bibsonomy.org/bibtex/2a5df51097a2fd476feca1271ad358448/biblio24},
	keywords = {immunoassay homogeneous immunoelectrode electrochemistry ecia ag_detection amperometry}
}

@article{citeulike:488379,
        title = {Multilabeling of ferrocenes to a glucose oxidase-digoxin conjugate for the development of a homogeneous electroenzymatic immunoassay.},
        address = {Department of Bioengineering, Tokyo Institute of Technology, Yokohama, Japan.},
        author = {T. Suzawa and Y. Ikariyama and M. Aizawa},
        journal = {Anal Chem},
        month = {November},
        number = 22,
        pages = {3889--3894},
        volume = 66,
        year = 1994,
        url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=7810897},
        id = {488379},
	issn = {0003-2700},
	priority = {2},
	abstract = {A new homogeneous electroenzymatic immunoassay was developed to determine antibody concentration using glucose oxidase and ferrocene as enzymatic and electrochemical amplifier, respectively. Digoxin (Dig)-conjugated glucose oxidase (GOx) was modified with ferrocene (Fec) to form Fec-GOx-Dig conjugate. After immunocomplex formation between the Fec-GOx-Dig conjugate and the anti-digoxin antibody, the complex underwent less electrochemical reaction due to the steric hindrance of the antibody. The ferrocene multilabeled conjugate was provided for the determination of anti-digoxin antibody. Since the strategy taken here is based on a combined effect of GOx and ferrocene, i.e., enzymatic amplification by GOx and electrochemical amplification by multilabeled ferrocenes, the antibody concentration was determined in the range from 1/50 to 1/500 dilution.},
	biburl = {http://www.bibsonomy.org/bibtex/2558850786f47348e4b8d8aa604ca5bcb/biblio24},
	keywords = {gox immunoassay ab_detection homogeneous ferrocene labeled_enzyme electrochemistry immunosensor ecia amperometry}
}