Conformational Changes in the α-subunit and Cation Transport by Pure Na, K-ATPase(MEMBRANE PROTEINS AND TRANSPORT-I)

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概要

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• In this study we examined the coupling of transitions between phosphoforms, E_1P and E_2P, of pure Na, K-ATPase to cation translocation after selective proteolysis of the α-subunit. Cleavage with trypsin at the carboxyl terminal side (Bond 1) of the aspartyl phosphate residue or with chymotrypsin at the aminoterminal side (Bond 1) blocks Na, K-ATPase and Na, K-transport, but the two splits have widely different effects on partial reactions. Cleavage of bond 3 blocks transition from E_1P to E_2P and abolish both (ADP+ATP)-Na/Na exchange and (ATP+Pi)-Rb/Rb exchange reactions in vesicles reconstituted with pure Na, K-ATPase. Cleavage of bond 1 interferes neither with the transitions nor with the exchange reactions. The results agree with the notion that the transitions between the phosphoforms, E_1P and E_2P, of the α-subunit are coupled to flipping of cation sites between inside exposed (E_1) and an outside exposed states (E_2).

• 東海大学の論文
• 1982-06-14

著者

• Jφrgensen Peter

  Institute Of Physiology University Of Aarhus

関連論文

• Ultrastructure of the Na, K-ion Pump(STRUCTURE OF MEMBRANE PROTEINS)
• Conformational Changes in the α-subunit and Cation Transport by Pure Na, K-ATPase(MEMBRANE PROTEINS AND TRANSPORT-I)

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