Characterization of the High-Affinity Verapamil Binding Site in a Plant Plasma Membrane Ca 2+ -selective Channel

1997 ◽  
Vol 157 (2) ◽  
pp. 139-145 ◽  
Author(s):  
M. Piñeros ◽  
M. Tester
Keyword(s):  
Plasma Membrane ◽  
Binding Site ◽  
High Affinity ◽  
Selective Channel ◽  
Plant Plasma Membrane

Characterization of a Specific, High Affinity [3H]Arginine8Vasopressin-Binding Site on Liver Microsomes from Different Strains of Rat and the Role of Magnesium*

Endocrinology ◽  
1986 ◽  
Vol 118 (3) ◽  
pp. 990-998 ◽  
Author(s):  
VENKAT GOPALAKRISHNAN ◽  
CHRIS R. TRIGGLE ◽  
PRAKASH V. SULAKHE ◽  
J. ROBERT McNEILL
Keyword(s):  
Binding Site ◽  
Liver Microsomes ◽  
High Affinity ◽  
Different Strains

scholarly journals Experimental and Theoretical Characterization of the High-Affinity Cation-Binding Site of the Purple Membrane

1998 ◽  
Vol 75 (2) ◽  
pp. 777-784 ◽  
Author(s):  
Leonardo Pardo ◽  
Francesc Sepulcre ◽  
Josep Cladera ◽  
Mireia Duñach ◽  
Amílcar Labarta ◽  
...  
Keyword(s):  
Binding Site ◽  
Purple Membrane ◽  
Cation Binding ◽  
High Affinity ◽  
Cation Binding Site ◽  
Theoretical Characterization

Large scale characterization of plant plasma membrane proteins

Biochimie ◽  
1999 ◽  
Vol 81 (6) ◽  
pp. 655-661 ◽  
Author(s):  
Véronique Santoni ◽  
Patrick Doumas ◽  
David Rouquié ◽  
Monique Mansion ◽  
Thierry Rabilloud ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Large Scale ◽  
Plasma Membrane Proteins ◽  
Scale Characterization ◽  
Plant Plasma Membrane

scholarly journals The Binding Site for Regulatory 14-3-3 Protein in Plant Plasma Membrane H+-ATPase

2003 ◽  
Vol 278 (43) ◽  
pp. 42266-42272 ◽  
Author(s):  
Anja T. Fuglsang ◽  
Jonas Borch ◽  
Katrine Bych ◽  
Thomas P. Jahn ◽  
Peter Roepstorff ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Binding Site ◽  
Plant Plasma Membrane

scholarly journals Characterization of a high-affinity and specific binding site for Gas6

FEBS Letters ◽  
1996 ◽  
Vol 387 (1) ◽  
pp. 75-77 ◽  
Author(s):  
Toru Nakano ◽  
Junji Kishino ◽  
Hitoshi Arita
Keyword(s):  
Binding Site ◽  
Specific Binding ◽  
High Affinity

Opioid receptors in bovine adrenal medulla

1984 ◽  
Vol 62 (10) ◽  
pp. 1284-1291 ◽  
Author(s):  
Michel Dumont ◽  
Simon Lemaire
Keyword(s):  
Binding Site ◽  
G Protein ◽  
Opioid Receptors ◽  
Opioid Peptides ◽  
Affinity Binding ◽  
Endogenous Opioid ◽  
High Affinity Binding ◽  
High Affinity ◽  
High Affinity Binding Site

Using prototypic ligands for each type of opioid receptors (μ, δ, κ, and σ) as well as compounds derived from each class of endogenous opioid peptides (β-endorphin, enkephalins, and dynorphins), we have undertaken the characterization of adrenomedullary opioid binding sites. The specific binding of [3H]etorphine ([3H]ET) to a membrane preparation of bovine adrenal medulla was greatly increased when the incubation temperature was raised from 22 to 37 °C. Characterization of the opioid binding sites was obtained at 37 °C with [3H]ET (nonspecific opioid ligand), [3H]ethylketocyclazocine ([3H]EKC; κ), [3H]dihydromorphine ([3H]DHM; μ), [3H]-[D-Ala2,D-Leu5]enkephalin ([3H]DADLE; δ), and N-[3H]allylnormetazocine ([3H]SKF-10047; σ) in the absence or presence of blocking agents for cross-reacting receptors. [3H]ET had a high affinity binding site (KD = 0.98 nM) with a Bmax of 119 pmol/g protein. All the other opioid compounds showed biphasic saturation curves with KD ranging from 0.6 to 1.29 nM for the high affinity binding site and from 2.49 to 12.1 nM for the low affinity binding site. The opioid μ-receptor was characterized by the high affinity binding site for [3H]DHM (KD = 1.29 nM; Bmax = 38 pmol/g protein). Blockade of the cross-reacting receptor sites for [3H]EKC, [3H]DADLE, and [3H]SKF-10047 revealed the presence of κ (KD = 0.66 nM; Bmax = 12 pmol/g protein), κ2 (benzomorphan site; KD = 11.1 nM; Bmax = 56 pmol/g protein), δ (KD = 0.67 nM; Bmax = 4.7 pmol/g protein), and σ (KD = 4.54 nM; Bmax = 32 pmol/g protein) opioid receptors. The ability of various opioid ligands to displace the binding of [3H]ET indicates a high potency for (−)-(1R,5R,9R,2″S)-5,9-dimethyl-2′-hydroxy-2-tetrahydrofurfuryl-6,7-benzomorphan hydrogen D-tartrate (MR-2034, a κ-opioid ligand; Ki = 6.2 nM), dihydromorphinone (DHMone; Ki = 6.9 nM), oxymorphone (Ki = 8.6 nM), DADLE (Ki high affinity = 8.4 nM) EKC (Ki = 31.8 nM), SKF-10047 (Ki = 75 nM), and opioid agonists/antagonists. trans-(+)-3,4-Dichloro-N-methyl-N-[2-(1-pyrrolidinyl)cyclohexyl]benzeneacetamide methanesulfonate hydrate (U-50,488H), the most specific κ-agonist, was a poor competitor (Ki = 5150 nM). However, the presence of κ-opioid receptors was supported by the ability of U-50,488H to displace [3H]EKC binding (Ki high affinity = 2.5 nM). The relative potency of various endogenous opioid peptides in displacing [3H]ET binding was as follows: β-endorphin [Formula: see text] dynorphin(1-17) > dynorphin(1-13) > [Arg6,Phe7)Met-enkephalin > Met-enkephalin > Leu-enkephalin. In addition, the presence of a high affinity binding site for dynorphin was demonstrated by the high potency of dynorphin (1-13) to displace [3H]EKC binding (Ki high affinity = 2.3 nM). These data provide further insights into the characterization of adrenal opioid receptors and suggest an in situ physiological role for adrenal opioid peptides.

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