Primary structure of porcine muscarinic acetylcholine receptor III and antagonist binding studies.
The complete amino acid sequence of porcine muscarinic acetylcholine receptor III has been deduced by cloning and sequencing the genomic DNA. The antagonist binding properties of muscarinic acetylcholine receptor III expressed from the cloned DNA in Xenopus oocytes correspond most closely to those of the pharmacologically defined M2 glandular (III) subtype.
Akiba
I
I
Department of Medical Chemistry, Faculty of Medicine, Kyoto University, Japan.
Kubo
T
T
Maeda
A
A
Bujo
H
H
Nakai
J
J
Mishina
M
M
Numa
S
S
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004274:DNA, Recombinant; D006031:Glycosylation; D008969:Molecular Sequence Data; D009116:Muscarine / Q000037:antagonists & inhibitors*; D009865:Oocytes / Q000378:metabolism; D010880:Piperidines / Q000378:metabolism; D010890:Pirenzepine / Q000031:analogs & derivatives / Q000378:metabolism; D011487:Protein Conformation; D011813:Quinuclidinyl Benzilate / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics; D051381:Rats; D011976:Receptors, Muscarinic / Q000235:genetics / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D013552:Swine; D014982:Xenopus laevis
D004274:DNA, Recombinant; D010880:Piperidines; D012333:RNA, Messenger; D011976:Receptors, Muscarinic; D010890:Pirenzepine; D011813:Quinuclidinyl Benzilate; D009116:Muscarine; C046773:hexahydrosiladifenidol; C048593:otenzepad