Isolation and characterization of the components of the sodium pump

1974 ◽  
Vol 7 (2) ◽  
pp. 239-274 ◽  
Author(s):  
Peter Leth Jørgensen
Keyword(s):  
Cell Membrane ◽  
Active Transport ◽  
Transport System ◽  
Sodium Pump ◽  
Enzyme System ◽  
Intact Cell ◽  
Test Tube ◽  
Isolation And Characterization ◽  
Sodium And Potassium

A satisfactory understanding of the functions of the sodium pump, the system responsible for the active transport of sodium and potassium, require the isolation and characterization of its protein and lipid components which are integrated in the structure of the cell membrane. The enzyme system (Na+ + K+)-ATPase, is located in membrane fragments and behaves in the test tube like the transport system in the intact cell membrane (Skou,1957) Purified preparations of this enzyme will contain some, if not all, of the components of the sodium pump.

Isolation and Characterization of a Monoclonal Antibody against Pig Kidney Sodium- and Potassium-Activated ATPase1

1985 ◽  
Vol 98 (1) ◽  
pp. 209-217 ◽  
Author(s):  
Osamu URAYAMA ◽  
Hideaki NAGAMUNE ◽  
Makoto NAKAO ◽  
Yukichi HARA ◽  
Hiroyuki SUGIYAMA ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Pig Kidney ◽  
Isolation And Characterization ◽  
Sodium And Potassium

The (Na++K+) activated enzyme system and its relationship to transport of sodium and potassium

1974 ◽  
Vol 7 (3) ◽  
pp. 401-434 ◽  
Author(s):  
Jens Chr. Skou
Keyword(s):  
Transport System ◽  
Enzyme System ◽  
Membrane Bound ◽  
Hydrolysis Of ◽  
Sodium And Potassium

It seems to be the membrane bound (Na++K+)-activated enzyme system which transforms the energy from a hydrolysis of ATP into a vectorial movement of sodium out and potassium into the cell against electrochemical gradients, i.e. this systems seems to be the transport system for sodium and potassium (see, for example, review by Skou, 1972; Hokin & Dahl, 1972).

Sodium and potassium movement in the excised rat aorta

1960 ◽  
Vol 199 (1) ◽  
pp. 28-30 ◽  
Author(s):  
Oswald Dawkins ◽  
David F. Bohr
Keyword(s):  
Cell Membrane ◽  
Active Transport ◽  
Rat Aorta ◽  
Rat Plasma ◽  
Electrolyte Composition ◽  
Krebs Solution ◽  
Equivalent Amount ◽  
Rapid Changes ◽  
Active Transport System ◽  
Sodium And Potassium

When the rat aorta is excised and placed in a bath of Krebs' solution it loses over two-thirds of its potassium and gains roughly an equivalent amount of sodium within the first 15 seconds. If the aorta is placed in rat plasma instead of Krebs' solution, a similar change occurs. These rapid changes in aorta electrolyte composition do not occur when the whole rat is perfused with Krebs' solution. It is concluded that in the handling involved in the removal of the aorta its cell membrane barriers are altered in such a way that they no longer maintain the normal transmembrane gradients of these cations. After 2 minutes in the bath the potassium in the aorta gradually increases and its sodium decreases suggesting that the cell membrane has regained its characteristics as a barrier and is capable of maintaining sodium and potassium gradients established by an active transport system.

Isolation and characterization of goat ovarian aromatase cDNA: assessment of the activity using an intact cell system and placental expression

2004 ◽  
Vol 62 (3-4) ◽  
pp. 532-543 ◽  
Author(s):  
Raúl José Bobes ◽  
Carolina Miranda ◽  
Mario Pérez-Martinez ◽  
Van Luu-The ◽  
Marta C Romano
Keyword(s):  
Intact Cell ◽  
Cell System ◽  
Isolation And Characterization

Isolation and characterization of a bacteriophage infective for a UDP-galactose-4-epimeraseless mutant of Escherichia coli

1975 ◽  
Vol 21 (8) ◽  
pp. 1217-1223 ◽  
Author(s):  
Christopher J. Pazoles ◽  
Charles F. Kulpa Jr.
Keyword(s):  
Escherichia Coli ◽  
Cell Membrane ◽  
Receptor Site ◽  
Bacterial Strains ◽  
Adsorption Studies ◽  
E Coli ◽  
Isolation And Characterization

A DNA bacteriophage, designated CP13, was isolated against Escherichia coli J5, a UDP-galactose-4-epimeraseless mutant of E. coli 0111:B4. Bacteriophage CP13 appears to be specific for rough bacterial strains. Adsorption studies with E. coli J5 grown with galactose show that the bacteriophage will not adsorb when complete lipopolysaccharide is present in the cell membrane. This indicates that lipopolysaccharide may be directly or indirectly involved with the receptor site for bacteriophage CP13. The bacteriophage DNA has a G + C content of 52%.

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