d-Glucose uptake by a rat liver plasma membrane preparation

1976 ◽  
Vol 443 (2) ◽  
pp. 254-266 ◽  
Author(s):  
W. Bachmann ◽  
D. Challoner
1983 ◽  
Vol 96 (1) ◽  
pp. 217-229 ◽  
Author(s):  
A L Hubbard ◽  
D A Wall ◽  
A Ma

A rat liver plasma membrane preparation was isolated and characterized both biochemically and morphologically. The isolation procedure was rapid, simple and effective in producing a membrane fraction with the following biochemical characteristics: approximately 40-fold enrichment in three plasma membrane markers, 5'-nucleotidase, alkaline phosphodiesterase I (both putative bile canalicular membrane enzymes), and the asialo-glycoprotein (ASGP) receptor (a membrane glycoprotein present along the sinusoidal front of hepatocytes); a yield of each of these plasma membrane markers that averaged approximately 16%; and minimal contamination by lysosomes, nuclei, and mitochondria, but persistent contamination by elements of the endoplasmic reticulum. Morphological analysis of the preparation revealed that all three major domains of the hepatocyte plasma membrane (sinusoidal, lateral, and bile canalicular) were present in substantial amounts. The identification of sinusoidal membrane was further confirmed when ASGP binding sites were localized predominantly to this membrane in the isolated PM using electron microscope autoradiography. By morphometry, the sinusoidal front membrane accounted for 47% of the total membrane in the preparation, whereas the lateral surface and bile canalicular membrane accounted for 6.8% and 23% respectively. This is the first report of such a large fraction of sinusoidal membrane in a liver plasma membrane preparation.


1972 ◽  
Vol 59 (11) ◽  
pp. 521-522 ◽  
Author(s):  
V. M. Govindan ◽  
H. Faulstich ◽  
Th. Wieland ◽  
B. Agostini ◽  
W. Hasselbach

1990 ◽  
Vol 265 (35) ◽  
pp. 21514-21519 ◽  
Author(s):  
P Blache ◽  
A Kervran ◽  
M Dufour ◽  
J Martinez ◽  
D Le-Nguyen ◽  
...  

1976 ◽  
Vol 154 (1) ◽  
pp. 11-21 ◽  
Author(s):  
J P Luzio ◽  
A C Newby ◽  
C N Hales

1. A rapid method for the isolation of hormonally sensitive rat fat-cell plasma membranes was developed by using immunological techniques. 2. Rabbit anti-(rat erythrocyte) sera were raised and shown to cross-react with isolated rat fat-cells. 3. Isolated rat fat-cells were coated with rabbit anti-(rat erythrocyte) antibodies, homogenized and the homogenate made to react with an immunoadsorbent prepared by covalently coupling donkey anti-(rabbit globulin) antibodies to aminocellulose. Uptake of plasma membrane on to the immunoadsorbent was monitored by assaying the enzymes adenylate cyclase and 5′-nucleotidase and an immunological marker consisting of a 125I-labelled anti-(immunoglobulin G)-anti-cell antibody complex bound to the cells before fractionation. Contamination of the plasma-membrane preparation by other subcellular fractions was also investigated. 4. By using this technique, a method was developed allowing 25-40% recovery of plasma membrane from fat-cell homogenates within 30 min of homogenization. 5. Adenylate cyclase in the isolated plasma-membrane preparation was stimulated by 5 μm-adrenaline.


1988 ◽  
Vol 23 (1) ◽  
pp. 19-24 ◽  
Author(s):  
Diana H. Petkova ◽  
Albena B. Momchilova-Pankova ◽  
Tania T. Markovska ◽  
Kamen S. Koumanov

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