Soluble and enzymatically stable (Na++K+)-ATPase from mammalian kidney consisting predominantly of protomer αβ-units von Brotherus, Jaakko R., Jacobsen, Lene, Jørgensen, Peter L.

Volltext

Detergent inactivation of sodium- and potassium-activated adenosinetriphosphatase of the electric eel von Brotherus, Jaakko R, Jost, Patricia C, Griffith, O. Hayes, Hokin, Lowell E

Volltext

Lipid-protein multiple binding equilibriums in membranes von Brotherus, Jaakko R, Griffith, O. Hayes, Brotherus, Martti O, Jost, Patricia C, Silvius, John R, Hokin, Lowell E

Volltext

Soluble and active renal Na,K-ATPase with maximum protein molecular mass 170,000 ± 9,000 daltons; formation of larger units by secondary aggregation von Brotherus, Jaakko R., Møller, Jesper V., Jørgensen, Peter L.

Volltext

Lipid--protein multiple binding equilibria in membranes von Brotherus, J R, Griffith, O H, Brotherus, M O, Jost, P C, Silvius, J R, Hokin, L E

Volltext

Charge Selectivity at the Lipid-Protein Interface of Membranous Na,K-ATPase von Brotherus, Jaakko R., Jost, Patricia C., Griffith, O. Hayes, John F. W. Keana, Hokin, Lowell E.

Volltext

Soluble and enzymatically stable [formula omitted] from mammalian kidney consisting predominantly of protomer αβ-units : Preparation, assay and reconstitution of active Na +, K +tr... von Brotherus, Jaakko R., Jacobsen, Lene, Jørgensen, Peter L.

Volltext

The active site and the phospholipid activation of rat liver lysosomal lipase are not stereospecific von Joutti, Anneli, Vainio, Petri, Brotherus, Jaakko R., Paltauf, F., Kinnunen, Paavo K.J.

Volltext