Estimation Of Serum Albumin

Estimation of Serum Albumin

Albumin is the most abundant serum protein produced by the liver. In clinical practice the serum level of albumin continues to be used as an important marker of the presence, progress or ofthe improvement of many diseases, even though it is the complex end result of synthesis, degradation a. nd distribution between intra- and extravascular space. The clinical history of albumin began as early as in 1837, when Ancell first recognized "albumen" and noted that this protein is needed for trans port functions, for maintaining fluidity of the vascular system and for the prevention of edema. However, the important physiological properties of serum proteins and their role in the regulation ofthe oncotic pressure were demonstrated later by the physiologist E. H. Starling in 1895. In 1917 the clinician A. A. Epstein first described the edema in patients with the nephro tic syndrome as being a result of a very low level of serum albumin. Al though the determination of serum albumin concentration became more popular after Howe in 1921 introduced the technique of separation of serum globulins from albumin by sodium sulfate, the first preparations of human serum albumin were made available for clinical use in only 1941 by the development of plasma fractionation by Cohn and his coworkers at Harvard Medical School.

A guide to the techniques and analysis of clinical data. Each of the seventeen sections begins with a drawing and biographical sketch of a seminal contributor to the discipline. After an introduction and historical survey of clinical methods, the next fifteen sections are organized by body system. Each contains clinical data items from the history, physical examination, and laboratory investigations that are generally included in a comprehensive patient evaluation. Annotation copyrighted by Book News, Inc., Portland, OR

Volume 1 of 2. Description of 144 methods of analysis for analytes commonly measured in a clinical chemistry laboratory

This book is a practical guidebook in biochemistry, for medical as well as life sciences' students. The book covers reference values, sample collection procedure and detailed protocol to perform experiments. Each experiment starts with a brief introduction of the protocol, followed by specimen requirements and procedure. The procedures are presented in a very lucid manner and discuss details of calculations and clinical interpretations,The book is divided into 29 chapters, It offers references, general guidelines and abbreviations and provides principles and procedures of clinical biochemistry tests, along with their diagnostic importance.

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Human serum albumin is found in the intravascular and extracellular space and is the main protein of human blood plasma. Human serum albumin binds water, cations (such as Ca2+, Na+, K+), fatty acids, hormones, bilirubin, thyroxin (T4) and pharmaceuticals. Structurally, the serum albumins are similar, each domain containing five or six internal disulfide bonds. In the opening chapter of Human Serum Albumin: Structure, Binding and Activity the authors review, the structure, content and binding of HSA.Then, the role of albumin in free radical trapping activities and as an oxyradical scavenger is described. A discussion of recent advances in the use of the antioxidant properties of human serum albumin to make drugs detectable in vivo is also presented.Human serum albumin has one tryptophan residue and shows a characteristic fluorescence of around 350 nm under ultraviolet irradiation. Because tryptophan is easily oxidized by reactive oxygen species and/or photoexcited molecules through electron transfer (leading to fluorescence diminishment) a fluorometry of this tryptophan residue is a useful tool to evaluate oxidation. In light of these characteristics, the authors examine the photosensitizing activity of organic photosensitizers, including porphyrins and phenothiazine dyes.The use of magnetic resonance imaging and spectroscopy for the determination of human serum albumin structure, drug binding and in vivo activity is explored, in addition to drug modifications using human serum albumin.Following this, this compilation studies the major approaches for the characterization of human serum albumin as a fluorinated drug delivery agent and fluorinated albumin influence on drug binding. Synthesis and characterization of fluorinated conjugates of albumin and adsorbed human serum albumin on surfaces containing CF3 are also discussed.The concluding study investigates possible similarities and differences in albumin concentration and the presence of tyrosine in urine from a population of healthy and microalbuminuria dependent women. The assessment of subtle changes in albumin concentration, the primary macromolecular component of urine, is critical for the diagnosis of early stage albuminuria, one of the major complications in nephropathy.

This book offers comprehensive information on the fundamentals and applications of ionic-liquid-based aqueous biphasic systems, which have predominantly (and successfully) been employed as alternative platforms for the extraction, separation and purification of diverse high-value products. The book consists of an initial introduction providing a brief overview, from fundamentals to applications, followed by nine chapters addressing the respective phase diagrams (interpretation and characterization) and remarkable examples of their applications. It also includes two final chapters focusing on recent developments in the search for more environmentally-benign and biocompatible ionic-liquid-based aqueous biphasic systems, and on the progress made to date concerning the recovery, recycling and reuse of the phase-forming components, the goal being the development of cost-effective and sustainable processes. The book offers an interesting and useful guide for a broad readership in the fields of green chemistry, biotechnology, chemical engineering, and biochemistry, among others. Mara G. Freire is a Coordinator Researcher at CICECO - Aveiro Institute of Materials, Chemistry Department, University of Aveiro, Portugal.

"Human serum albumin is a protein in the blood with a molecular mass 66.5 kDa. In this study, was developed a method for determination of human serum albumin protein as monomer and its aggregates using a size exclusion column and HPLC instrument. Optimum conditions of the method were flow rate 0.2 ml/min, injection volume of the sample with concentration 5 mg/ml was 0.2 μl, column temperature 30 °C, wavelength 214 nm. Mobile phase was sodium phosphate at concentration 150 mM and pH 7 using an isocratic elution. The method is validated in term of linearity, precision robustness, specificity, system suitability test and stability."--