Pig kidney Na⁺,K⁺‐ATPase

Abstract

(Na+ + K+)‐ATPase α‐Subunit β‐Subunit cDNA nucleotide sequence Primary structure Glycopeptide Transmembrane arrangement

Immunodetection of Na,K‐ATPase α3‐isoform in renal and nerve tissues

“…The comparison of the primary structures derived from the nucleotide sequences of o~ [11], + [12] and ~3 [4] revealed the notable difference in two regions ( fig. 1).…”

“…The same height of the upper plateau on titration curves demonstrates the identical antigen quantity in three binding processes. This can be explained by nonspecific interaction of aBSA-I antibodies and the Na,K-ATPase ce-subunit region (227-236) 227 236 E E E P QNDNL Y o~-subunit [11] \ IIII…”

Detailed structural analysis of exposed domains of membrane‐bound Na+, K+‐ATPase A model of transmembrane arrangement

“…Calculation of the hydrophobicity profile of the a-subunit allowed the prediction of eleven probable transmembrane clusters [1,3]: 89-l 14, 123-142., 284-306, 313-341, 530-554, 569-597, 780-803, 842-867, 909-930, 946-971, 973-994. Previously, we established conditions for trypsinolysis of the membrane-bound enzyme (0.1 N NH4HCO3, pH 7.3; 1% trypsin, 10 min), providing exhaustive hydrolysis of the exposed regions of the polypeptide chain of the catalytic subunit [3,12].…”

“…Previously, we established conditions for trypsinolysis of the membrane-bound enzyme (0.1 N NH4HCO3, pH 7.3; 1% trypsin, 10 min), providing exhaustive hydrolysis of the exposed regions of the polypeptide chain of the catalytic subunit [3,12]. Among the water-soluble peptides isolated from the hydrolysate we identified three fragments, viz.…”

“…Most of the information concerning the exposed portions of the catalytic subunit had been obtained previously from structural analysis of the extramembrane peptides formed on selective tryptic hydrolysis of the m-subunit entering the membrane-bound enzyme [1,3,12]. The membrane moiety of the hydrolysate, being a unique composition of membrane segments of the a-subunit and intact glycoprotein, became an object for studying the exposed domains of the latter.…”