Absence of hexokinase activity in plasma membranes of morris hepatoma 5123 t.c.

1971 ◽  
Vol 44 (6) ◽  
pp. 1443-1448 ◽  
Author(s):  
R.S. Bhatty ◽  
R.A. Hickie
FEBS Letters ◽  
1975 ◽  
Vol 49 (3) ◽  
pp. 346-349 ◽  
Author(s):  
Ornella Dionisi ◽  
Tommaso Galeotti ◽  
Tullio Terranova ◽  
Paola Arslan ◽  
Angelo Azzi

1975 ◽  
Vol 64 (1) ◽  
pp. 367-375 ◽  
Author(s):  
Ann M. Dnistrian ◽  
Vladimir P. Skipski ◽  
Marion Barclay ◽  
Edward S. Essner ◽  
C. Chester Stock

FEBS Letters ◽  
1984 ◽  
Vol 168 (2) ◽  
pp. 241-244 ◽  
Author(s):  
Reinhard Neumeier ◽  
Ulrike Dethlefs ◽  
Werner Reutter

FEBS Letters ◽  
1984 ◽  
Vol 169 (2) ◽  
pp. 169-173 ◽  
Author(s):  
T. Galeotti ◽  
S. Borrello ◽  
G. Palombini ◽  
L. Masotti ◽  
M.B. Ferrari ◽  
...  

2006 ◽  
Vol 1123 (2) ◽  
pp. 205-211 ◽  
Author(s):  
James G. Clifton ◽  
Mari Kino Brown ◽  
Feilei Huang ◽  
Xuesong Li ◽  
Werner Reutter ◽  
...  

2007 ◽  
Vol 849 (1-2) ◽  
pp. 293-301 ◽  
Author(s):  
James G. Clifton ◽  
Xuesong Li ◽  
Werner Reutter ◽  
Douglas C. Hixson ◽  
Djuro Josic

1980 ◽  
Vol 190 (1) ◽  
pp. 51-55 ◽  
Author(s):  
P Vischer ◽  
W Reutter

Half-lives and rate constants of degradation of protein-bound fucose have been determined in plasma membranes and total cell homogenates of rat liver and Morris hepatoma 7777. The existence of at least two dynamically different classes of fucose-containing glycoproteins could be demonstrated in both liver and hepatoma plasma membranes. The apparent half-lives were 8.4 and 24.5 h (host liver) and 11.5 and 33.9 h (Morris hepatoma). Since this biphasic loss of fucose residues was not observed for sialic acid [Harms & Reutter (1974) Cancer Res. 34, 3165–3172], the differences are possibly related to specific functions of fucosylated glycoproteins of the plasma membrane.


Author(s):  
G. Zampighi ◽  
M. Kreman

The plasma membranes of most animal cells contain transport proteins which function to provide passageways for the transported species across essentially impermeable lipid bilayers. The channel is a passive transport system which allows the movement of ions and low molecular weight molecules along their concentration gradients. The pump is an active transport system and can translocate cations against their natural concentration gradients. The actions and interplay of these two kinds of transport proteins control crucial cell functions such as active transport, excitability and cell communication. In this paper, we will describe and compare several features of the molecular organization of pumps and channels. As an example of an active transport system, we will discuss the structure of the sodium and potassium ion-activated triphosphatase [(Na+ +K+)-ATPase] and as an example of a passive transport system, the communicating channel of gap junctions and lens junctions.


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