Structural interactions of globular proteins—Bovine serum albumin, egg albumin, and lysozyme, in aqueous medium, elucidated with molar volumes, viscosities, energy functions, and IR spectra from 293.15 to 303.15 K

2006 ◽  
Vol 103 (3) ◽  
pp. 1420-1429 ◽  
Author(s):  
Man Singh
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Ir Spectra ◽  
Aqueous Medium ◽  
Bovine Serum ◽  
Globular Proteins ◽  
Energy Functions ◽  
Molar Volumes ◽  
Egg Albumin ◽  
Structural Interactions

scholarly journals Antibodies in sulfonamide-induced immune thrombocytopenia recognize calcium-dependent epitopes on the glycoprotein IIb/IIIa complex

Blood ◽  
1994 ◽  
Vol 84 (1) ◽  
pp. 176-183 ◽  
Author(s):  
BR Curtis ◽  
JG McFarland ◽  
GG Wu ◽  
GP Visentin ◽  
RH Aster
Keyword(s):  
Flow Cytometry ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Aqueous Medium ◽  
Bovine Serum ◽  
Immune Thrombocytopenia ◽  
Acetyl Derivative ◽  
Igg Antibodies ◽  
Calcium Dependent ◽  
Drug Dependent

Abstract Drug-dependent IgG antibodies (DDAb) induced by sulfamethoxazole (SMX) and sulfisoxazole (SIX) were identified by flow cytometry in 15 patients who developed thrombocytopenia while taking one of these medications. Fourteen of the 15 DDAb were specific solely for the glycoprotein (GP)IIb/IIIa complex, and 13 of these reacted wholly or in part with epitopes present only on the intact GPIIb/IIIa heterodimer. None of 12 SMX-induced DDAb cross-reacted with SIX, but one of three SIX-induced antibodies reacted with SMX. Each of 10 SMX-induced DDAb tested reacted with the N1-acetyl metabolite of SMX, but only one reacted fully with the N4-acetyl derivative. Detection of the SMX- and SIX-dependent antibodies was facilitated by using bovine serum albumin (BSA) to achieve suspension of these weakly soluble drugs in an aqueous medium. Our findings indicate that DDAb induced by SMX and SIX, in contrast to those induced by quinidine and quinine, are mainly specific for GPIIb/IIIa and react preferentially with calcium-dependent epitopes present only on the intact GPIIb/IIIa heterodimer.

scholarly journals Pharmacological and ADMET-based pharmacokinetic properties of Syzygium samarangense var. parviflorum leaf extract in in vitro, in vivo and in silico models

2020 ◽  
Vol 48 (3) ◽  
pp. 1155-1175
Author(s):  
Rahni HOSSAIN ◽  
Md A. RAHMAN ◽  
Md. K. J. RAFI ◽  
Tanvir A. SIDDIQUE ◽  
Abdullah A. NOMAN ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Computational Models ◽  
Clot Lysis ◽  
Pharmacological Properties ◽  
Reference Drug ◽  
Egg Albumin ◽  
Anti Inflammatory

This research investigated pharmacological properties mainly the anti-inflammatory, anthelmintic, thrombolytic and anxiolytic potential of methanol extract of Syzygium samarangense (MESS) var. parviflorum. Anti-inflammatory action by bovine serum albumin, egg albumin denaturation and membrane stabilization, anthelmintic by live parasites, thrombolytic by clot lysis and anxiolytic by elevated plus maze (EPM) and light and dark box (LDB) tests were measured. The four targeted pharmacological properties were further justified using the most prevalent compounds, isolated from this plant, to be undergone for their pharmacokinetic property’s analyses, sitemap analyses and lignad-receptor interactions by computational models through SwissADME and Schrödinger, 2018 softwares against PDB 6COX, 6D6T, 1JFF receptors. MESS was found to display statistically significant (P < 0.05) inhibition of Bovine Serum albumin and Egg albumin denaturation compared to reference drug diclofenac sodium. Remarkable vermicidal effect on the paralysis and death of anthelmintic parasites was observed at MESS concentration 200 mg/dL. A nondescript clot lysis of MESS compared to streptokinase was evident in in vitro thrombolytic assay. MESS increased the number of times the animal crossed from one compartment to the other and the time spent in the brightly-lit chamber of the LDB. Three-methylchalcone derivatives out of seven MESS compounds were undertaken, based on cut off value and sitemap prediction score, for further ligand-receptor binding efficiency. All these three compounds showed promising docking score, glide emodel and glide energy against PDB 6COX, 6D6T and 1DDJ, plasmin proteins demonstrating the prospects of MESS to be materialized for anti-inflammatory, anthelmintic, and thrombolytic therapeutics with further clarification.

Sign in / Sign up

Export Citation Format

Share Document