In vitro Binding of Nitracrine to DNA in Chromatin

1989 ◽  
Vol 44 (3-4) ◽  
pp. 307-311 ◽  
Author(s):  
Dorota Wilmańska ◽  
Leszek Szmigiero ◽  
Marek Gniazdowski
Keyword(s):  
Reference Compound ◽  
Physiological Conditions ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Initial Decrease ◽  
Partial Dissociation ◽  
Sulfhydryl Compounds ◽  
Relative Accessibility ◽  
Apparent Influence

Abstract In the presence of sulfhydryl compounds nitracrine, an anticancer drug, binds covalently to DNA . The accessibility of DNA in chromatin both to nitracrine and to 8-methoxypsoralen. which was used as a reference compound in this study, when assayed in NaCl concentrations from 0 to 2 m show similar characteristics. The initial decrease reaches a minimum at 0.15 m NaCl above which dissociation of non-histone proteins and histones at higher ionic strengths is demonstrated by an increase in accessible sites. The relative accessibility of DNA in chromatin to nitracrine is, however, lower than that found for 8-methoxypsoralen. Partial dissociation of chromatin with 0.7 m NaCl increases the accessibility of DNA in chromatin when assayed in the absence of NaCl but has no apparent influence when estimated at ionic strength close to physiological conditions.

Methyl 3β-(4-[125I]Iodophenyl)Tropane-2β-Carboxylate In Vitro Binding to Dopamine and Serotonin Transporters Under “Physiological” Conditions

2008 ◽  
Vol 62 (3) ◽  
pp. 978-986 ◽  
Author(s):  
Marc Laruelle ◽  
Suzanne S. Giddings ◽  
Yolanda Zea-Ponce ◽  
Dennis S. Charney ◽  
John L. Neumeyer ◽  
...  
Keyword(s):  
Serotonin Transporters ◽  
Physiological Conditions ◽  
In Vitro Binding ◽  
Vitro Binding

scholarly journals In vitro Binding Capacity of Wheat and Barley for Mn, Zn, Cu and Fe

2015 ◽  
Vol 9 (6) ◽  
pp. 56-60 ◽  
Author(s):  
Ali Ghodrat ◽  
Akbar Yaghobfar ◽  
Yahya Ebrahimnezhad ◽  
Habib Aghdam Shahryar ◽  
Abolfazl Ghorbani
Keyword(s):  
Small Intestine ◽  
Binding Capacity ◽  
Total Carbohydrate ◽  
Total Dietary Fiber ◽  
Physiological Conditions ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Two Samples ◽  
Mineral Binding

This study was carried out to determination of in vitro binding capacity of wheat and barley for Mn, Zn, Cu and Fe. For this reason wheat and barley were chemical analyzed for moisture, protein, ash, ether extract, total carbohydrate, NDF, ADF, ADL, crude fiber, viscosity, cellulose, hemicelluloses, total dietary fiber, and endogenous minerals. Mineral binding capacity of two samples for Mn, Zn, Fe, and Cu under sequential simulated physiological conditions of the stomach, small intestine, and colon was investigated and compared. Barley showed the higher mineral binding capacity in small intestine. Among the minerals, Fe exhibited the highest percentage of binding under the simulated physiological conditions of the small intestine and the lowest percentage of removing occurred in the stomach for both cereals. Cereals had an affinity for Fe>Cu>Zn>Mn. 

Discovery of New AKT1 Inhibitors by Combination of In silico Structure Based Virtual Screening Approaches and Biological Evaluations

2019 ◽  
Author(s):  
Filip Fratev ◽  
Denisse A. Gutierrez ◽  
Renato J. Aguilera ◽  
suman sirimulla
Keyword(s):  
Virtual Screening ◽  
Success Rate ◽  
Protein Interactions ◽  
In Silico ◽  
Biological Data ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Screening Protocol ◽  
Screening Approaches

AKT1 is emerging as a useful target for treating cancer. Herein, we discovered a new set of ligands that inhibit the AKT1, as shown by in vitro binding and cell line studies, using a newly designed virtual screening protocol that combines structure-based pharmacophore and docking screens. Taking together with the biological data, the combination of structure based pharamcophore and docking methods demonstrated reasonable success rate in identifying new inhibitors (60-70%) proving the success of aforementioned approach. A detail analysis of the ligand-protein interactions was performed explaining observed activities.<br>

scholarly journals ADP-ribosylation of integrin α7 modulates the binding of integrin α7β1 to laminin

2004 ◽  
Vol 385 (1) ◽  
pp. 309-317 ◽  
Author(s):  
Zhefeng ZHAO ◽  
Joanna GRUSZCZYNSKA-BIEGALA ◽  
Anna ZOLKIEWSKA
Keyword(s):  
C2c12 Myotubes ◽  
Post Translational Modification ◽  
Integrin Β1 ◽  
Adp Ribosylation ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
C2c12 Skeletal Muscle Cells ◽  
Adp Ribosyltransferase

The extracellular domain of integrin α7 is ADP-ribosylated by an arginine-specific ecto-ADP-ribosyltransferase after adding exogenous NAD+ to intact C2C12 skeletal muscle cells. The effect of ADP-ribosylation on the structure or function of integrin α7β1 has not been explored. In the present study, we show that ADP-ribosylation of integrin α7 takes place exclusively in differentiated myotubes and that this post-translational modification modulates the affinity of α7β1 dimer for its ligand, laminin. ADP-ribosylation in the 37-kDa ‘stalk’ region of α7 that takes place at micromolar NAD+ concentrations increases the binding of the α7β1 dimer to laminin. Increased in vitro binding of integrin α7β1 to laminin after ADP-ribosylation of the 37-kDa fragment of α7 requires the presence of Mn2+ and it is not observed in the presence of Mg2+. In contrast, ADP-ribosylation of the 63-kDa N-terminal region comprising the ligand-binding site of α7 that occurs at approx. 100 μM NAD+ inhibits the binding of integrin α7β1 to laminin. Furthermore, incubation of C2C12 myotubes with NAD+ increases the expression of an epitope on integrin β1 subunit recognized by monoclonal antibody 9EG7. We discuss our results based on the current models of integrin activation. We also hypothesize that ADP-ribosylation may represent a mechanism of regulation of integrin α7β1 function in myofibres in vivo when the continuity of the membrane is compromised and NAD+ is available as a substrate for ecto-ADP-ribosylation.

IC-P-199: Comparing [3 H]MK-6240 and [3 H]AV-1451(T-807) In In vitro Binding Studies in Brain Tissues

2016 ◽  
Vol 12 ◽  
pp. P144-P144
Author(s):  
Zhizhen Zeng ◽  
Patricia J. Miller ◽  
Brett M. Connolly ◽  
Stacey S. O’Malley ◽  
Idriss Bennacef ◽  
...  
Keyword(s):  
Binding Studies ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Brain Tissues

In vitro binding properties and autoradiographic imaging of 3-iodobenzamide ([125I]-IBZM): A potential imaging ligand for D-2 dopamine receptors in spect

Life Sciences ◽  
1988 ◽  
Vol 42 (21) ◽  
pp. 2097-2104 ◽  
Author(s):  
Thomas Brücke ◽  
Yuan Feen Tsai ◽  
Catherine McLellan ◽  
Weerachai Singhanyom ◽  
Hank F. Kung ◽  
...  
Keyword(s):  
Dopamine Receptors ◽  
Binding Properties ◽  
In Vitro Binding ◽  
Vitro Binding

Specific in vitro binding of (S,S)-[3H]MeNER to norepinephrine transporters

Synapse ◽  
2005 ◽  
Vol 56 (2) ◽  
pp. 100-104 ◽  
Author(s):  
Subroto Ghose ◽  
Masahiro Fujita ◽  
Paul Morrison ◽  
George Uhl ◽  
Dennis L. Murphy ◽  
...  
Keyword(s):  
In Vitro Binding ◽  
Vitro Binding
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