Your browser doesn't support javascript.
loading
Polypeptide components of the apamin receptor associated with a calcium activated potassium channel.
Leveque, C; Marqueze, B; Couraud, F; Seagar, M.
Affiliation
  • Leveque C; Laboratoire de Biochimie, CNRS UA1179, Faculté de Médecine Nord, Marseille, France.
FEBS Lett ; 275(1-2): 185-9, 1990 Nov 26.
Article in En | MEDLINE | ID: mdl-2175714
Photoaffinity labeling of rat brain membranes with [125I]ANPAA-apamin incorporated radioactivity into polypeptides of 86 and 59 kDa and occasionally a more weakly labeled component of 45 kDa. These polypeptides were immunoprecipitated with anti-apamin antibodies and treated with glycosidases. Neither the 86 nor the 59 kDa polypeptide appeared to be N-glycosylated. Partial proteolytic mapping of affinity labeled polypeptides with chymotrypsin or V8 protease generated an identical pattern. These results suggest that the 59 and 45 kDa components are not additional subunits of an oligomeric protein but result from cleavage of the 86 kDa polypeptide.
Subject(s)
Search on Google
Database: MEDLINE Main subject: Apamin / Synaptic Membranes / Potassium Channels / Receptors, Neurotransmitter Type of study: Risk_factors_studies Limits: Animals Language: En Journal: FEBS Lett Year: 1990 Type: Article Affiliation country: France
Search on Google
Database: MEDLINE Main subject: Apamin / Synaptic Membranes / Potassium Channels / Receptors, Neurotransmitter Type of study: Risk_factors_studies Limits: Animals Language: En Journal: FEBS Lett Year: 1990 Type: Article Affiliation country: France