In vitro Binding of MX2 (KRN8602) and Epirubicin to Human Plasma Protein

Pharmacology ◽  
1997 ◽  
Vol 55 (6) ◽  
pp. 279-284
Author(s):  
Wei-zheng. Zhang ◽  
Walter Cosolo ◽  
John Zalcberg
Keyword(s):  
Human Plasma ◽  
Plasma Protein ◽  
In Vitro Binding ◽  
Human Plasma Protein ◽  
Vitro Binding

The effect of free fatty acids on the in-vitro binding of testosterone in human plasma

1993 ◽  
Vol 136 (2) ◽  
pp. 327-330 ◽  
Author(s):  
M. J. Diver
Keyword(s):  
Fatty Acids ◽  
Free Fatty Acids ◽  
Pregnant Women ◽  
Human Plasma ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Significant Difference

ABSTRACT The effect of supraphysiological levels of free fatty acids (FFA) on the binding of testosterone to sex-hormone binding globulin (SHBG) and on non-SHBG binding in both male plasma and plasma from pregnant women was studied. Six FFAs were added to plasma as individual acids. No alteration in testosterone binding to SHBG could be demonstrated with any of the FFAs in either male plasma or plasma from pregnant women. When the same plasma was heated to destroy SHBG binding, a highly significant (P <0·01) increase in non-SHBG binding was seen in both male plasma and plasma from pregnant women when the unsaturated FFAs oleic, linoleic and linolenic acids were added. No significant difference was demonstrated with the saturated FFAs, palmitic, stearic and arachidic acids. Journal of Endocrinology (1993) 136, 327–330

Photobinding of some 7-chloro-1,4-benzodiazepines to human plasma protein in vitro and photopharmacology of diazepam in the rat

1988 ◽  
Vol 10 (3) ◽  
pp. 122-129 ◽  
Author(s):  
A. Bakri ◽  
G. M. J. Beijersbergen Van Henegouwen ◽  
H. De Vries
Keyword(s):  
Human Plasma ◽  
Plasma Protein ◽  
Human Plasma Protein

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.

scholarly journals A western blot approach to detection of human plasma protein conjugates derived from D-penicillamine.

1994 ◽  
Vol 53 (4) ◽  
pp. 256-260 ◽  
Author(s):  
C A Laycock ◽  
M J Phelan ◽  
R C Bucknall ◽  
J W Coleman
Keyword(s):  
Western Blot ◽  
Human Plasma ◽  
Plasma Protein ◽  
Protein Conjugates ◽  
Human Plasma Protein
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