نتایج جستجو برای: prene chhic human serum albumin protein hsa

تعداد نتایج: 2688079  

Journal: :journal of paramedical sciences 0
alireza ahmadzadeh faculty of medicine, shahid beheshti university of medical sciences, tehran, iran. seyed mohammad mahdavi proteomics research center, shahid beheshti university of medical sciences, tehran, iran. parviz karimi faculty of medicine, tehran university of medical sciences, tehran, iran abdolrahim nikzamir faculty of medicine, shahid beheshti university of medical sciences, tehran, iran.

advanced glycation end-products (ages) are formed by non-enzymatic reaction between reducing sugar and protein. ages play important roles in pathogenesis of diabetic, aging complications, endothelial dysfunction and neurological diseases such as the alzheimer’s disease. therefore compounds that prevent the glycation reaction are purported to have therapeutic effect on patients with diabetes and...

Human serum albumin (HSA) is the most abundant protein in the blood plasma. Molecular dynamics simulations of subdomain IIA of HSA and its complex with salicylic acid (SAL) were performed to investigate structural changes induced by the ligand binding. To estimate the binding affinity of SAL molecule to subdomains IB and IIA in HSA protein, binding free energies were calculated using the Molecu...

Journal: :Journal of The Serbian Chemical Society 2021

The binding of a popular food supplement and well-known antioxidant, dihydro-alpha-lipoic acid (DHLA) to human serum albumin (HSA) was characterised. monitored by several spectroscopic methods together with the molecular docking approach. HSA able bind DHLA moderate affinity, 1.00?0.05?104 M-1. Spectroscopic data demonstrated that preferential site for on is IIA (Sudlow I). Both experimental an...

2016
Ralph Adams Laura Griffin Joanne E. Compson Mark Jairaj Terry Baker Tom Ceska Shauna West Oliver Zaccheo Emma Davé Alastair DG. Lawson David P. Humphreys Sam Heywood

We generated an anti-albumin antibody, CA645, to link its Fv domain to an antigen-binding fragment (Fab), thereby extending the serum half-life of the Fab. CA645 was demonstrated to bind human, cynomolgus, and mouse serum albumin with similar affinity (1-7 nM), and to bind human serum albumin (HSA) when it is in complex with common known ligands. Importantly for half-life extension, CA645 binds...

Human serum albumin (HSA) is the most abundant protein in the blood plasma. Drug binding to HSA is crucial to study the absorption, distribution, metabolism, efficiency and bioavailability of drug molecules. In this study, isothermal titration calorimetry and molecular dynamics simulation of HSA and its complex with indometacin (IM) were performed to investigate thermodynamics parameters and th...

Journal: :Photochemistry and photobiology 1993
C Dughi N V Bhagavan D M Jameson

Familial dysalbuminemic hyperthyroxinemia (FDH) is an autosomal dominant syndrome in which clinically euthyroid patients have elevated total thyroxine levels. These high serum thyroxine levels are traceable to altered binding of thyroxine to the patient's albumin. Albumin from FDH patients and normal volunteers have been purified. Reverse-phase and ion-exchange high performance liquid chromatog...

Journal: :iranian journal of medical sciences 0
daryoush amanat

background: possibility to trace-label albumin with isotopes results in information concerning its synthesis, breakdown, and distribution in the intra and extra cellular spaces. the iodination of albumin is a widespread procedure used in scientific studies. bromine not only is more reactive and less expensive than iodine, but bonds more easily with many elements. therefore, it could be a suitab...

Journal: :Biophysica 2022

In this paper, the quartz crystal microbalance with dissipation monitoring (QCM-D) was used to investigate hydrophobicity and binding strength (KD) for 10 different drugs interacting human serum albumin (HSA). Quantitative structure activity relationship (QSAR) analysis determine between drug (ClogP) HSA log(1/KD). The results are compared prior knowledge on bovine (BSA) binding. We demonstrate...

Journal: :Nucleic acids research 1981
R M Lawn J Adelman S C Bock A E Franke C M Houck R C Najarian P H Seeburg K L Wion

A recombinant plasmid has been constructed which contains the mature protein coding region of the human serum albumin (HSA) gene. Bacteria containing this plasmid synthesize HSA protein under control of the E. coli trp promoter-operator. The DNA sequence and predicted protein sequence of HSA were determined from the cDNA plasmid and are compared to existing data obtained from direct protein seq...

A. Divsalar A.A. Saboury H. Mansuri-Torshizi M. Evini S. Khodabakhshian

Human serum albumin (HSA) is an abundant, multifunctional and nonglycosylated negatively charged plasma protein. HSA ascribed ligand-binding and transport properties, antioxidant functions and enzymatic activities. In the present study, the interaction and side effects of a new designed anti-cancer compound (1,10-phenanthroline butyl dithiocarbamato palladium(II) nitrate) on HSA have been inves...

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