Specific binding sites for corticosterone in isolated cells and plasma membrane from rat liver

1991 ◽  
Vol 120 (2) ◽  
pp. 115-124 ◽  
Author(s):  
Miguel Trueba ◽  
Iñaki Ibarrola ◽  
Kepa Ogiza ◽  
Aida Marino ◽  
José María Macarulla
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Binding Sites ◽  
Specific Binding ◽  
Isolated Cells ◽  
Specific Binding Sites

Characterization of Specific Binding Sites for Corticosterone in Mouse Liver Plasma Membrane

1989 ◽  
Vol 8 (4) ◽  
pp. 229-239 ◽  
Author(s):  
Miguel Trueba ◽  
IÑAki Ibarrola ◽  
Ana Isabel Vallejo ◽  
MarÍA José Sancho ◽  
Aida Marino ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Binding Sites ◽  
Mouse Liver ◽  
Specific Binding ◽  
Liver Plasma Membrane ◽  
Specific Binding Sites

scholarly journals Specific binding sites for inositol 1,3,4,5-tetrakisphosphate are located predominantly in the plasma membranes of human platelets

1994 ◽  
Vol 298 (3) ◽  
pp. 739-742 ◽  
Author(s):  
P J Cullen ◽  
Y Patel ◽  
V V Kakkar ◽  
R F Irvine ◽  
K S Authi
Keyword(s):  
Plasma Membrane ◽  
Binding Sites ◽  
Plasma Membranes ◽  
Human Platelet ◽  
Specific Binding ◽  
Human Platelets ◽  
Intracellular Membranes ◽  
Specific Binding Sites ◽  
Carrier Free ◽  
Membrane Location

In the present study we describe the characterization and localization of Ins(1,3,4,5)P4-binding sites in human platelet membranes. Specific binding sites for Ins(1,3,4,5)P4 have been identified on mixed, plasma and intracellular membranes from neuraminidase-treated platelets using highly purified carrier-free [32P]Ins(1,3,4,5)P4. The displacement of Ins(1,3,4,5)P4 from these sites by Ins(1,4,5)P3 and InsP6 occurs at greater than two orders of magnitude higher concentrations and with Ins(1,3,4,5,6)P5 at about 40-fold higher concentrations than with Ins(1,3,4,5)P4. The membranes were further separated by free-flow electrophoresis into plasma and intracellular membranes. The Ins(1,3,4,5)P4-binding sites separated with plasma membranes, and showed similar affinities and specificities as mixed membranes, whereas Ins(1,4,5)P3-binding sites were predominantly in the intracellular membranes. These results suggest a predominantly plasma membrane location for putative Ins(1,3,4,5)P4 receptors in human platelets.

scholarly journals Characterization of a thyroid-hormone-binding site on nuclear envelopes and nuclear matrices of the male-rat liver

1984 ◽  
Vol 219 (3) ◽  
pp. 1001-1007 ◽  
Author(s):  
Y A Lefebvre ◽  
J T Venkatraman
Keyword(s):  
Rat Liver ◽  
Binding Sites ◽  
Intact Animal ◽  
Binding Capacity ◽  
Specific Binding ◽  
Male Rat ◽  
Scatchard Analysis ◽  
Specific Binding Sites ◽  
Number Of Binding Sites

Nuclear envelopes and nuclear matrices were isolated from the male-rat liver. Incubation of 125I-labelled 3,3′,5-tri-iodothyronine (T3) with the nuclear-envelope fraction resulted in specific binding of T3 to the membranes. Maximum specific binding occurred at 30 degrees C after 2h incubation. Storage for 1 week at -80 degrees C resulted in no loss of binding. Scatchard analysis revealed a class of binding sites with KD 86 nM. 3,3′,5′-Tri-iodothyronine was as effective a competitor of [125I]T3 binding to nuclear envelopes as was L-T3 itself, and tri-iodothyroacetic acid was 70% as potent as T3. L- and D-thyronine did not compete for [125I]T3 binding. Incubation of nuclear envelopes with 0.6 M-NaCl before addition of T3 resulted in the complete loss of specific binding sites, whereas exposure of the membranes to 2.0 M-NaCl after incubation with T3 did not extract binding sites. Nuclear matrices, after incubation with [125I]T3 under the same conditions, were shown to possess a class of binding sites with a similar KD but with approx. 30% of the maximum binding capacity. Nuclear envelopes from hypothyroid animals may possess slightly lower numbers of binding sites compared with nuclear envelopes from the intact animal, whereas nuclear matrices from hypothyroid animals have the same number of binding sites as do nuclear envelopes from the intact animal. In conclusion, nuclear envelopes and nuclear matrices have a class of binding sites with relatively high affinity for T3. It is distinct from nuclear and cytosolic binding sites.

SPECIFIC BINDING SITES FOR L-TRIIODOTHYRONINE IN RAT LIVER AND KIDNEY CYTOSOL

1976 ◽  
Vol 82 (1) ◽  
pp. 98-104 ◽  
Author(s):  
T. J. Visser ◽  
H. F. Bernard ◽  
R. Docter ◽  
G. Hennemann
Keyword(s):  
Rat Liver ◽  
Binding Sites ◽  
Specific Binding ◽  
Specific Binding Sites ◽  
Liver And Kidney
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