Serum Albumin

The first of its kind, All About Albumin summarizes the chemistry, genetics, metabolism, clinical implications, and commercial aspects of albumin. It provides the most up-to-date sequences, structures, and compositions of many species, and includes more than 2000 references. Includes up-to-date sequences, structures, and compositions of many species Reviews the protein chemistry, genetic control, and metabolism of albumin Covers medical and cell culture applications in vivo and in vitro, with a section on handling albumin in the laboratory Presents the relationship of albumin to its superfamily with an updated scheme for their evolution First complete coverage of all aspects of serum albumin in one volume, with more than 2000 references

It is only during the last decade that the functions of sinusoidal endothelial cells, Kupffer cells, hepatic stellate cells, pit cells and other intrahepatic lymphocytes have been better understood. The development of methods for isolation and co-culturing various types of liver cells has established that they communicate and cooperate via secretion of various intercellular mediators. This monograph summarizes multiple data that suggest the important role of cellular cross-talk for the functions of both normal and diseased liver. Special features of the book include concise presentation of the majority of detailed data in 19 tables. Original schemes allow for the clear illustration of complicated intercellular relationships. This is the first ever presentation of the newly emerging field of liver biology, which is important for hepatic function in health and disease and opens new avenues for therapeutic interventions.

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.

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.

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

Serum albumin is a large protein present in cow serum protein (BSA, Bovine Serum Albumin) rich in essential amino acids and compounds with disulfide bridges and thiol groups. This protein passes into breast milk from the bloodstream by diffusion, has antioxidant capacity and protects fats from oxidation. Albumin has the ability to inhibit tumor factors and bind to fat, mobilize them in the body to perform other functions such as obtaining energy or forming membranes. It is also able to block the conversion of angiotensin I into angiotensin II (vasoconstrictor) which gives it antihypertensive action. In addition, it has the ability to reduce cholesterol absorption, complex heavy metals and is an opioid agonist (acts on opioid receptors and promotes analgesia). BSA is the most studied and produced protein worldwide in the last 80 years. This protein brings large dividends to the world economy with a very prominent and favorable annual growth at a cost of 100 USD per gram. This book brings new contributions to the science and industry of this biopolymer. The audience of this book is very wide from students, teachers and researchers (doctors, pharmacists, biochemists and industrialists of this sector). Therefore, this book has a great future and many readers to whom it is addressed.

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.