Characterization of specific binding sites for high-density lipoproteins on rat hepatocytes: Effects of estradiol and testosterone

1996 ◽  
Vol 122 (6) ◽  
pp. 1194-1198
Author(s):  
T. G. Vishnyakova ◽  
A. V. Bocharov ◽  
I. N. Baranova ◽  
V. S. Repin
Keyword(s):  
Binding Sites ◽  
Specific Binding ◽  
Rat Hepatocytes ◽  
High Density ◽  
High Density Lipoproteins ◽  
Specific Binding Sites

Characterization of specific binding sites for PAF in the iris and ciliary body of rabbit

1989 ◽  
Vol 160 (1) ◽  
pp. 250-256 ◽  
Author(s):  
M.T. Domingo ◽  
P.E. Chabrier ◽  
J.L. Van Delft ◽  
N.L. Verbeij ◽  
N.J. Van Haeringen ◽  
...  
Keyword(s):  
Binding Sites ◽  
Ciliary Body ◽  
Specific Binding ◽  
Specific Binding Sites

scholarly journals Characterization of the liver P2-purinoceptor involved in the activation of glycogen phosphorylase

1986 ◽  
Vol 240 (2) ◽  
pp. 367-371 ◽  
Author(s):  
S Keppens ◽  
H De Wulf
Keyword(s):  
Binding Sites ◽  
Glycogen Phosphorylase ◽  
Plasma Membranes ◽  
Specific Binding ◽  
Rank Order ◽  
Rat Hepatocytes ◽  
Isolated Hepatocytes ◽  
Isolated Rat Hepatocytes ◽  
P2 Purinoceptors

Evidence has been presented for the existence in rat liver of P2-purinoceptors which are involved in the control of glycogenolysis. Isolated rat hepatocytes and purified liver plasma membranes have been used to study the binding of the ATP analogue adenosine 5′-[alpha- [35S]thio]triphosphate (ATP alpha [35S]) to these postulated P2-purinoceptors. The nucleotide analogue behaves as a full agonist for the activation of glycogen phosphorylase in isolated hepatocytes, 0.3 microM being required for half-maximal activation. Specific binding of ATP alpha [35S] to hepatocytes and plasma membranes occurs within 1 min and is essentially reversible. The analysis of the dose-dependency at equilibrium indicates the presence of binding sites with Kd of 0.23 microM with hepatocytes and Kd of 0.11 microM with plasma membranes. The relative affinities of 10 nucleotide analogues were deduced from competition experiments for ATP alpha [35S] binding to hepatocytes, and these correlated highly with their biological activity (activation of glycogen phosphorylase in hepatocytes). For all the agonists, binding occurs in the same concentration range as the biological effect. These data clearly suggest that the detected binding sites correspond to the physiological P2-purinoceptors involved in the regulation of liver glycogenolysis. The rank order of potency of some ATP analogues suggests that liver possesses the P2Y-subclass of P2-purinoceptors.

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 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.

scholarly journals Solubilization and characterization of substance P-binding sites from chick brain membranes

1988 ◽  
Vol 252 (2) ◽  
pp. 545-551 ◽  
Author(s):  
H P Too ◽  
M R Hanley
Keyword(s):  
Substance P ◽  
Binding Sites ◽  
Specific Binding ◽  
Chick Brain ◽  
High Concentration ◽  
Brain Membrane ◽  
Brain Membranes ◽  
Specific Binding Sites ◽  
Octyl Glucoside

Sites binding monoiodinated-Bolton-Hunter-reagent-labelled substance P were solubilized from 1-day-old-chick brain membrane by using non-ionic detergents (1% digitonin/1% n-octyl glucoside) and a high concentration of NaCl (0.5 M). The solubilized preparation retained the pharmacological properties of the high-affinity binding sites found in the native membrane. The high density of specific binding sites (approximately 2 pmol of binding sites/mg of protein) suggests that the chick brain membranes may be a useful source for the purification of the substance P-binding sites.

Sign in / Sign up

Export Citation Format

Share Document