In vitro binding capacities and physicochemical properties of soluble fiber prepared by microfluidization pretreatment and cellulase hydrolysis of peach pomace

LWT ◽  
2015 ◽  
Vol 63 (1) ◽  
pp. 677-684 ◽  
Author(s):  
Honggao Xu ◽  
Qiong Jiao ◽  
Fang Yuan ◽  
Yanxiang Gao
Keyword(s):  
Physicochemical Properties ◽  
Soluble Fiber ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Hydrolysis Of ◽  
Cellulase Hydrolysis

scholarly journals Phospholipase C–mediated hydrolysis of PIP2 releases ERM proteins from lymphocyte membrane

2009 ◽  
Vol 184 (3) ◽  
pp. 451-462 ◽  
Author(s):  
Jian-Jiang Hao ◽  
Yin Liu ◽  
Michael Kruhlak ◽  
Karen E. Debell ◽  
Barbara L. Rellahan ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Phospholipase C ◽  
Membrane Association ◽  
Erm Proteins ◽  
Cytoskeletal Remodeling ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Hydrolysis Of

Mechanisms controlling the disassembly of ezrin/radixin/moesin (ERM) proteins, which link the cytoskeleton to the plasma membrane, are incompletely understood. In lymphocytes, chemokine (e.g., SDF-1) stimulation inactivates ERM proteins, causing their release from the plasma membrane and dephosphorylation. SDF-1–mediated inactivation of ERM proteins is blocked by phospholipase C (PLC) inhibitors. Conversely, reduction of phosphatidylinositol 4,5-bisphosphate (PIP2) levels by activation of PLC, expression of active PLC mutants, or acute targeting of phosphoinositide 5-phosphatase to the plasma membrane promotes release and dephosphorylation of moesin and ezrin. Although expression of phosphomimetic moesin (T558D) or ezrin (T567D) mutants enhances membrane association, activation of PLC still relocalizes them to the cytosol. Similarly, in vitro binding of ERM proteins to the cytoplasmic tail of CD44 is also dependent on PIP2. These results demonstrate a new role of PLCs in rapid cytoskeletal remodeling and an additional key role of PIP2 in ERM protein biology, namely hydrolysis-mediated ERM inactivation.

The physicochemical properties, in vitro binding capacities and in vivo hypocholesterolemic activity of soluble dietary fiber extracted from soy hulls

2016 ◽  
Vol 7 (12) ◽  
pp. 4830-4840 ◽  
Author(s):  
Chun Liu ◽  
Xiao-Lu Lin ◽  
Zhili Wan ◽  
Yuan Zou ◽  
Fen-Fen Cheng ◽  
...  
Keyword(s):  
Physicochemical Properties ◽  
Dietary Fiber ◽  
Soluble Dietary Fiber ◽  
In Vitro Binding ◽  
Soy Hull ◽  
Vitro Binding ◽  
Soy Hulls

Soy hull soluble dietary fiber possessed favorablein vitrobinding capacities andin vivohypocholesterolemic activity.

Drug Adsorption to Charcoals and Anionic Binding Resins

1990 ◽  
Vol 9 (2) ◽  
pp. 95-97 ◽  
Author(s):  
A.H. Al-Shareef ◽  
D.C. Buss ◽  
P.A. Routledge
Keyword(s):  
Molecular Weight ◽  
Physicochemical Properties ◽  
Adsorption Capacity ◽  
Maximum Adsorption Capacity ◽  
Physiochemical Properties ◽  
In Vitro Binding ◽  
Drug Adsorption ◽  
Consistent Relationship ◽  
Vitro Binding

1. The in-vitro binding of four drugs with differing physiochemical properties to two commercial charcoal preparations and two anionic binding resins was studied at 37°C and pH 7.4. 2. The two charcoal preparations (Carbomix and Medicoal) behaved similarly and adsorbed metoclopramide and antipyrine to a greater degree than warfarin or paracetamol. 3. Cholestyramine had a significantly greater maximum adsorption capacity (K2) for warfarin and significantly lower adsorption capacity for paracetamol and metoclopramide than did the charcoals. 4. Colestipol behaved similarly but also bound metoclopramide to a significantly greater extent than did either cholestyramine or charcoal and antipyrine to a significantly lesser extent than did Carbomix. 5. There appeared to be no consistent relationship between the maximum adsorption capacity of the adsorbents for the drugs tested and the physicochemical properties of those drugs (e.g. basic or acidic structure, p Ka or molecular weight).

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
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