Pig kidney Na+,K+-ATPase. Primary structure and spatial organization.
cDNAs complementary to pig kidney mRNAs coding for alpha- and beta-subunits of Na+,K+-ATPase were cloned and sequenced. Selective tryptic hydrolysis of the alpha-subunit within the membrane-bound enzyme and tryptic hydrolysis of the immobilized isolated beta-subunit were also performed. The mature alpha- and beta-subunits contain 1016 and 302 amino acid residues, respectively. Structural data on the peptides from extramembrane regions of the alpha-subunit and on glycopeptides of the beta-subunit underlie a model for the transmembrane arrangement of Na+,K+-ATPase polypeptide chains.
Ovchinnikov YuA
Modyanov
N N
NN
Broude
N E
NE
Petrukhin
K E
KE
Grishin
A V
AV
Arzamazova
N M
NM
Aldanova
N A
NA
Monastyrskaya
G S
GS
Sverdlov
E D
ED
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002462:Cell Membrane / Q000201:enzymology; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004247:DNA / Q000235:genetics; D007679:Kidney Medulla / Q000201:enzymology*; D008051:Lipid Bilayers; D008565:Membrane Proteins; D009693:Nucleic Acid Hybridization; D010446:Peptide Fragments; D011061:Poly A / Q000235:genetics; D012313:RNA / Q000235:genetics; D012333:RNA, Messenger / Q000235:genetics; D000254:Sodium-Potassium-Exchanging ATPase / Q000235:genetics; D013552:Swine
D008051:Lipid Bilayers; D008565:Membrane Proteins; D010446:Peptide Fragments; D012333:RNA, Messenger; D011061:Poly A; D012313:RNA; D004247:DNA; D000254:Sodium-Potassium-Exchanging ATPase