Biochemical enrichment and biophysical characterization of a taste receptor for L-arginine from the catfish, <Emphasis Type="Italic">Ictalurus puntatus</Emphasis> |
| |
| Authors: | William?Grosvenor Yuri?Kaulin Andrew?I?Spielman Douglas?L?Bayley D?Lynn?Kalinoski John?H?Teeter Email author" target="_blank">Joseph?G?BrandEmail author |
| |
| Institution: | (1) Monell Chemical Senses Center, 19104-3308 Philadelphia, PA, USA;(2) Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russia;(3) New York University College of Dentistry, 10010 New York, NY, USA;(4) Institute of Neurological Sciences, University of Pennsylvania, 19104 Philadelphia, PA, USA;(5) Veterans Affairs Medical Center, 19104 Philadelphia, PA, USA;(6) Department of Biochemistry, School of Dental Medicine, University of Pennsylvania, 19104 Philadelphia, PA, USA;(7) Department of Pathology, Anatomy & Cell Biology, Thomas Jefferson University, 19107-6799 Philadelphia, PA, USA;(8) UCSD Thornton Hospital, 92037 San Diego, CA, USA |
| |
| Abstract: | Background The channel catfish, Ictalurus punctatus, is invested with a high density of cutaneous taste receptors, particularly on the barbel appendages. Many of these receptors
are sensitive to selected amino acids, one of these being a receptor for L-arginine (L-Arg). Previous neurophysiological and
biophysical studies suggested that this taste receptor is coupled directly to a cation channel and behaves as a ligand-gated
ion channel receptor (LGICR). Earlier studies demonstrated that two lectins, Ricinus communis agglutinin I (RCA-I) and Phaseolus vulgaris Erythroagglutinin (PHA-E), inhibited the binding of L-Arg to its presumed receptor sites, and that PHA-E inhibited the L-Arg-stimulated
ion conductance of barbel membranes reconstituted into lipid bilayers. |
| |
| Keywords: | |
| 本文献已被 SpringerLink 等数据库收录！ |
|
