Premium
Polypeptide components of the apamin receptor associated with a calcium activated potassium channel
Author(s) -
Leveque Christian,
Marqueze Beatrice,
Couraud Francois,
Seagar Michael
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81468-4
Subject(s) - apamin , calcium activated potassium channel , potassium channel , chemistry , calcium , potassium , sk channel , receptor , biophysics , n type calcium channel , calcium channel , medicine , endocrinology , biochemistry , t type calcium channel , ion channel , biology , organic chemistry
Photoaflinity labeling of rat brain membraines with [ 125 l]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 b %glycoxylated. Partial protocolytic mapping of affinity labeled polypeptides with chymotrypsin or V8 protease generated an identical pattern. Thes results suggest that the 59 and 45 kDa components are not additional subunits of an oligomeric protein but results from cleavage of the 86 kDa polypeptide