Study Of Conformational Stability Of Human Serum Albumin Compared To Nitrated Human Serum Albumin Using Uv

"The interaction of Human Serum Albumin with Thymoquinone plays an important role in the pharmacology and pharmacodynamics in order to help us better understand the absorption and distribution of Thymoquinone in the body. This study showed that Human Serum Albumin as a model protein for elucidating Human Serum Albumin with Thymoquinone complex at different temperatures. Also we estimated the conformational stability, of Human Serum Albmin and its complex with Thymoquinonr against the urea action."

Abstract: The structural changes in human serum albumin upon its binding of fatty acid anions were investigated. Red-shifts in HSA's UV spectrum following the addition of long chain fatty acid (LCFA) anions reflect a major change in its conformation. Similar but smaller changes after the addition of decanoate and other medium chain-length fatty acid (MCFA) anions reflect either a smaller or a less complete conformation change. Dansylsarcosine's fluorescence, is sharply reduced by low levels of MCFA anions known to bind to the same site. Similar levels of LCFA anions have only a small effect on its fluorescence but suppress it at higher levels. Prominent and characteristic spectral changes accompanying PLP's reaction with fatty acid-free HSA are only slightly affected by four equivalents of LCFA anion but almost completely eliminated by five equivalents. Similar levels of MCFA anions have little affect on PLP's reaction with HSA but gradually suppress it at higher levels. These results appear to reflect a concerted change in HSA's conformation upon the simultaneous binding of five LCFA anions. Isothermal titrations with LCFA and MCFA anions suggest the former bind cooperatively whereas the latter do not. The thiol content of fresh plasma HSA undergoes a biphasic decrease. The initial rapid phase was partially inhibited by superoxide dismutase, catalase, a mixture of both, to a lesser extent by allopurinol, and to a still lesser extent by EDTA, suggesting it is due mainly due to the reaction of Cys-34 of HSA in plasma with reactive oxygen species (especially hydrogen peroxide and superoxide) and free cysteine, cysteinylglycine and reduced glutathione in plasma. The S-nitroso derivatives of glutathione, N-acetyl-penicillamine, L-cysteine, 3-mercaptopropionic acid and 2-mercaptoethanol were shown to react with bovine oxyhemoglobin at different rates and with different kinetics. When RSNOs were in excess, they were shown to participate in both the transnitrosation reaction with the -SH groups of â Cys93 and the oxidation reaction with the hemes of oxyhemoglobin, which when combined with results from the Saville assay indicating the production of S-nitrosylated protein(s), suggested that excess RSNOs react with HbO2 â chains with two pathways and with á chains with only one pathway.

This book presents a comprehensive overview of medical and pharmaceutical applications of human serum albumin (HSA), with updates on structural aspects of albumin from the perspectives of X-ray crystallography and NMR, endogenous and exogenous ligand binding of albumin in various pathological conditions, and genetic variants and their phenotypes. Rapid progress and development of its applications have resulted in outstanding results for which albumin has clearly been proven to be a robust biomaterial. Contributions from leading international experts in this field show how HSA is applied to diagnosis, therapy, drugs, and treatment, with a comprehensive introduction of HSA. This volume will appeal to scientists in pharmaceutical and medical research including pharmaceutical chemists, pharmacokineticists, toxicologists, and biochemists not only in academia but also in industry. Readers can effectively acquire the most recent knowledge of applications of HSA and its impact on human health in a single volume.

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Serum Albumin (HSA) is a plasma protein of great significance with an ability to bind nerous endogenous and exogenous ligands, having a single polypeptide chain of 585 amino constructed in three domains of relatively equal size. Although HSA's existence has been own for many years, its characterisation and ability to bind ligands still remain enigmatic. Only 11992 was the crystal structure of HSA reported (Carter and Ho, 1992). Effective crystallisation I the determination of meaningful crystallographic data and structure had proven difficult. The I report concerned HSA crystals grown using zero gravity conditions. i objective of this project is the characterisation of recombinant and native HSA using Ultra-Diet (UV) & circular dichroism spectroscopy (CD) and involved HSA conformational changes, hich altered the ability to bind or off-load ligands. Changing environment, together with the use F characteristic "marker ligands," influences binding to provide a handle that can be utilised and litored. This enables the assignment of binding sites and the study of perturbating conditions. jing conditions such as pH, temperature, ionic strength and solvents in the presence and of ligands were employed to extract further information on this elusive protein, tients of recombinant HSA were also used (namely domain I and domain I + II) under tical conditions as the whole protein in order to help elucidate and assign binding sites.

Albumin Structure, Function and Uses reviews the many facets of serum albumin, including its history and evolutionary development, structure and function, synthesis, degradation, distribution and transport, and metabolic behavior. The use, misuse, and abuse of albumin in the treatment of disease are also discussed. This book is comprised of 17 chapters and begins with a commentary on how albumin is used, misused, and abused in the treatment of disease such as peptic ulcer, and a description of the real indications for its use. Concepts in albumin purification are then examined, along with the amino acid sequence of serum albumin and some aspects of its structure and conformational properties. Subsequent chapters explore the phylogenetics of albumin; albumin binding sites; clinical implications of drug-albumin interaction; genetics of human serum albumin; and hepatic synthesis of export proteins. Albumin catabolism and intracellular transport are also considered, together with surgical and clinical aspects of albumin metabolism. This monograph should be a useful resource for biochemists and clinicians.