Journal article
Bispecific antibody modification of nicotinic acetylcholine receptors for biosensing
Biosensors & bioelectronics, Vol.11(1), pp.91-102
1996
Handle:
https://hdl.handle.net/2376/115573
PMID: 8600918
Abstract
Recent results show that bispecific antibodies can be used to tailor the selectivity of nicotinic acetylcholine receptors for biosensing purposes. The nicotinic acetylcholine receptors reconstituted in bilayer lipid membranes are inactivated when two bispecific antibodies, attached to the same receptor, bind to a single antigen molecule. Experiments with patch clamp recording equipment reveal that antigen levels of 10
−8 M completely and irreversibly inactivate small numbers of nicotinic acetylcholine receptors. This approach may lead to the construction of biosensors capable of detecting individual antibody-antigen (Ab-Ag) binding events.
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Details
- Title
- Bispecific antibody modification of nicotinic acetylcholine receptors for biosensing
- Creators
- Steven R ReikenBernard J Van WieHimawan SutisnaDavid F MoffettAlan R KochMoris SilberWilliam C Davis - Department of Veterinary Microbiology & Pathology, Washington State University, Pullman, WA 99164-7040, USA
- Publication Details
- Biosensors & bioelectronics, Vol.11(1), pp.91-102
- Academic Unit
- Veterinary Microbiology and Pathology, Department of; Chemical Engineering and Bioengineering, School of
- Publisher
- Elsevier B.V
- Identifiers
- 99900548287601842
- Language
- English
- Resource Type
- Journal article