SERUM ALBUMIN

Serum albumin

CAS NO . :   70024-90-7
EC/LIST NO.:  274-272-6 

Serum albumin, often referred to simply as blood albumin, is an albumin (a type of globular protein) found in vertebrate blood. 
Human serum albumin is encoded by the ALB gene.
Other mammalian forms, such as bovine serum albumin, are chemically similar.

Serum albumin is produced by the liver, occurs dissolved in blood plasma and is the most abundant blood protein in mammals. 
Serum albumin is essential for maintaining the oncotic pressure needed for proper distribution of body fluids between blood vessels and body tissues; without albumin, the high pressure in the blood vessels would force more fluids out into the tissues. 
Serum albumin also acts as a plasma carrier by non-specifically binding several hydrophobic steroid hormones and as a transport protein for hemin and fatty acids. 
Too much or too little circulating serum albumin may be harmful. 
Serum albumin in the urine usually denotes the presence of kidney disease. 
Occasionally albumin appears in the urine of normal persons following long periods of standing (postural albuminuria).

Serum albumin; It is the most important serum protein that lowers metals, ions, fatty acids, amino acids, metabolites, enzymes, hormones and oncotic. 
Serum album life 17-26 and results are also synthesized. A small amount of albumin in it is excreted in the urine, also catabolized. 
Serum albumin makes up about 45-55% of the total protein. The albumin/globulin ratio is between 1-2.5. 
Normal Values ​​3.8-5.4/dl Compatibility of albumin to albumin: 
Rarely, serum specification is increased. Art may be due to dehydration, not a specific disease. 
Due to Hypergate of Albumin: Hypergammaglobulinemia of Malabsorption Toxins of Analgeule Malnutrition, starvation, amino acid cirrhosis Malignant hypothyroidism Sep Alcohol administration tr Myocardial Nephrotic syndrome Weakening enteropathies in rheumatoid arthritis Chronic education Eclampsia.

Serum albumin (also called human albumin), which is in the plasma part of the blood, is a type of protein synthesized by the liver, approximately 12 to 14 grams per day. 
Serum albumin is the most abundant of the 3 basic protein types in the blood.

Serum albumin is effective in regulating the density of blood, which is mostly water, and plays an important role in the exchange between organs and tissues through the blood. 
In other words, albumin allows the large protein molecules in the plasma part of the blood to pass through narrow areas such as capillaries in all parts of the body and regulates the oncotic pressure.

Serum albumin is a protein made by your liver. 
Serum albumin helps keep fluid in your bloodstream so it doesn't leak into other tissues. 
Serum albumin also carries a variety of substances throughout your body, including hormones, vitamins, and enzymes.
Low albumin levels may indicate a problem with your liver or kidneys.

Serum albumin (Fig. 14.11) is the most abundant protein in blood and is also the major carrier of free fatty acids in blood. 
Upon binding to serum albumin, the concentration of total fatty acids in blood is ∼1 mM while its concentration in the surrounding aqueous solution is a 1000-fold less. 
In addition to fatty acids, serum albumin can nonspecifically bind steroids, thyroid hormones, hemin, and other odd molecules . 
Serum albumin is a water-soluble, anionic globular protein of molecular weight ∼65,000. 
The protein's structure is dominated by several long α-helices that make the protein rigid . 
Serum albumin houses 11 distinct hydrophobic binding domains and so is capable of simultaneously carrying multiple fatty acids.

Serum albumin is a protein that is produced in the liver. 
Serum albumin enters the bloodstream where it helps carry vitamins, enzymes, and other important substances. 
Serum albumin also helps prevent fluids from leaking out of the bloodstream.

An albumin blood test measures the amount of albumin in a sample of your blood. 
Serum albumin can be used to help identify various health conditions, including problems that affect the liver and kidney.

Serum albumin is a multi-functional protein that is able to bind and transport numerous endogenous and exogenous compounds. 
The development of albumin drug carriers is gaining increasing importance in the targeted delivery of cancer therapy, particularly as a result of the market approval of the paclitaxel-loaded albumin nanoparticle, Abraxane. 
Considering this, there is renewed interest in isolating and characterizing albumin-binding proteins or receptors on the plasma membrane that are responsible for albumin uptake. 
Initially, the cellular uptake and intracellular localization of albumin was unknown due to the large confinement of the protein within the vascular and interstitial compartment of the body.
Studies have since assessed the intracellular localization of albumin in order to understand the mechanisms and pathways responsible for its uptake, distribution and catabolism in multiple tissues, and this is reviewed herein.

serum albumin, protein found in blood plasma that helps maintain the osmotic pressure between the blood vessels and tissues. 
Serum albumin accounts for 55 percent of the total protein in blood plasma.
Circulating blood tends to force fluid out of the blood vessels and into the tissues, where it results in edema (swelling from excess fluid). 
The colloid nature of albumin—and, to a lesser extent, of other blood proteins called globulins—keeps the fluid within the blood vessels.
Serum albumin also acts as a carrier for two materials necessary for the control of blood clotting: 
antithrombin, which keeps the clotting enzyme thrombin from working unless needed, and  heparin cofactor, which is necessary for the anticlotting action of heparin. 
The serum albumin level falls and rises in such liver disorders as cirrhosis or hepatitis. 
Transfusions of serum albumin are used to combat shock and whenever it is necessary to remove excess fluid from the tissues. 
Similar albumin compounds with other functions occur in plants, animal tissues, egg whites, and milk

Serum albumin is a protein produced in the liver and found in excess in the blood. 
The album has the task of making an exchange between tissues and organs using the blood path. 
The high or low value of albumin in the blood causes various diseases and some problems.

About 12 to 14 grams of albumin is produced daily by the liver. 
Serum albumin, which creates a balance between the blood and fluids and tissue, also carries some molecules in the blood to the cells. 
Large proteins cannot pass through narrow vessels and cell membranes. 
Serum albumin provides oncotic pressure and allows large molecules and proteins to pass through this narrow space.

This pressure provided by albumin prevents the accumulation of fluid in the vascular bed and therefore the risk of edema formation, while preventing the rise in blood pressure. 
In addition, albumin provides the transport of fatty acids, which are difficult to dissolve in water, vitamin B6, thyroid hormones and drugs used in the blood. 
Serum albumin also retains substances that pose a danger to the body.

The most abundant protein in the plasma part of the blood is albumin. 
Serum albuminmeasurement tests can be measured by two different methods, urine and blood. 
The normal range of albumin in the blood of an adult is 3.4 to 5.4 g/dl. 
The normal range of albumin in the urine of an adult is 0 to 8 mg/dl.

Having a value below the normal value ranges for albumin in a laboratory test is called low albumin. 
Low albumin causes edema in the person's body. 
Insufficient level of albumin can be caused by reasons such as insufficient production of albumin in the liver, albumin degradation and albumin degradation to a large extent. 
Liver diseases such as hepatitis, cirrhosis and excessive alcohol consumption also cause insufficient synthesis of albumin in the liver.
Serum albumin is possible.

Although Serum albumin is a rare condition, the presence of albumin above the normal value range is called albumin elevation. 
Serum albumin elevation generally occurs due to lack of fluid. 
Serum albumin may occur due to the use of diuretic drugs, diabetes, excessive sweating, diarrhea and albumin intake via blood.

Diabetes can cause both a decrease and an increase in albumin levels. 
This happens when diabetes leads to excess fluid excretion in the body and leads to protein leaks in the kidneys.

Serum albumin is the main protein that's found in our blood. 
Serum albumin's made in our liver, but we need a very good diet with enough protein to make the right amount. 
The normal level of albumin in the blood is 3.5 g/dL to 5 g/dL.

Serum albumin has many important jobs. 
Serum albumin acts like a magnet in the blood to keep fluid in the right place throughout your body. 
When Serum albumin's too low, you may get swelling from the build up of fluid in your feet, ankles, hands, around your eyes, lower back, or other parts of your body.

Albumin also carries important substances throughout the body, like hormones and drugs. 
So when serum albumin is low, these important products can't get to where they are needed in your body.

Serum albumin can be low in the blood for these reasons:

Liver disease
Extra fluid in your blood due to problems like heart failure. 
This extra fluid makes your albumin level seem low, even though it may be normal.
Poor nutrition
Stress, which can cause inflammation throughout your body.
Losing albumin in the urine

Eat a well-balanced diet with the right amount of protein. 
But not only do you need enough protein from foods like eggs and nuts, you also need enough energy from carbohydrate foods like whole grain bread and rice.
Control albuminuria. You healthcare team may tell you to take a special type of blood pressure medicine, either an ACEi (angiotensin converting enzyme inhibitor) or an ARB (angiotensin receptor blocker). 
You should also follow a diet low in salt and sodium.
Control fluid build-up in your body. 
Your healthcare team may tell you to take a drug called a diuretic to remove extra fluid in your body. 
You should also follow a diet low in salt and sodium.
Make sure that your healthcare team has checked your liver.
Your healthcare team may tell you to take dietary supplements that give you extra protein and calories.
Depending on the reason for your low serum albumin, your healthcare team may give you albumin through a needle in a vein (IV albumin).

Serum albumin is the most abundant protein in human blood. 
Serum albumin is produced in the liver and has a serum half-life of approximately 19 days. 
Transporting a large variety of hydrophobic substances like fatty acids, drugs and metabolites is one of its main physiological functions. 
Beside this Serum albumin maintains the oncotic pressure and buffers the pH of the blood.

Albumin consists of 585 amino acids, arranged in three mainly helical subunits (I, II, III) each divided into two subdomains (A, B).
For long chain fatty acids seven binding sites are known, three of them with high and four with lower affinity.

In recent years low molecular weight biomarkers bound to serum carrier proteins like albumin were intensively investigated assuming they might have a potential for early disease detection.

Serum albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones in the blood and plays a major role in stabilizing extracellular fluid volume by contributing to oncotic pressure (known also as colloid osmotic pressure) of plasma.

Because smaller animals (for example rats) function at a lower blood pressure, they need less oncotic pressure to balance this, and thus need less albumin to maintain proper fluid distribution.

Serum albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. 
The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin

Serum albumin is a globular, water-soluble, un-glycosylated serum protein of approximate molecular weight of 65,000 Daltons.

Serum albumin (when ionized in water at pH 7.4, as found in the body) is negatively charged. 
The glomerular basement membrane is also negatively charged in the body; some studies suggest that this prevents the filtration of albumin in the urine. 
According to this theory, that charge plays a major role in the selective exclusion of albumin from the glomerular filtrate. 
A defect in this property results in nephrotic syndrome leading to albumin loss in the urine. 
Nephrotic syndrome patients are sometimes given albumin to replace the lost albumin.

serum albumin (SA) is also known as ALB, which is the main protein of plasma and has a good binding capacity for water,Ca2+,Na+,K+,fatty acids,hormones, bilirubin and drugs.
The main function of SA is the regulation of the colloidal osmotic pressure of blood. 
As Major zinc transporter in plasma, SA typically binds about 80% of all plasma zinc. 
A variant structure of albumin could lead to increased binding of zinc resulting in an asymptomatic augmentation of zinc concentration in the blood. 
Defects in serum albumin can cause familial dysalbuminemic hyperthyroxinemia which is a form of euthyroid hyperthyroxinemia that is due to increased affinity of serum albumin for T4. 
Serum albumin is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.

Blood is a vital fluid that circulates in our veins in a constant order and forms the basis of life. 
Blood consists of 55% plasma, which is blood fluid, and 45% blood cells.

Plasma:Serum albumin is the liquid part of the blood. 
Serum albumin is a mixture of water, sugar, fat, protein and salts.

In the structure of the plasma; There are 90% water, 8% protein, 0.9% inorganic salts, 1.1% other organic compounds.

This 8% protein contains 60% albumin, 36% globulin, and 4% fibrinogen.

If the albumin level is below the reference value, it is defined as low albumin. 
Large protein molecules in the blood plasma of a person with low albumin cannot pass through narrow vessel structures. 
The reason for this is that the amount of albumin is not at a level to balance the oncotic pressure. 
Therefore, edema occurs, which can be defined as fluid accumulation in body tissues. 
Swelling due to edema occurs especially in the wrists and ankles, legs, face and eyelids. 
Low albumin may be caused by insufficient synthesis of albumin in the liver, excessive albumin loss and albumin degradation. 
Excessive alcohol use, cirrhosis, hepatitis, and some other liver diseases may cause albumin not to be synthesized sufficiently by the liver. 
In addition, nutritional disorders such as diabetes, stomach ulcers, some chronic and rheumatic diseases, hypothyroidism, hypoadrenalism, growth hormone disorders, being confined to bed and prolonged fasting may cause a decrease in albumin level in the blood. 
Conditions that increase albumin loss can be seen in the presence of bleeding, diarrhea, traumas, burns, celiac disease and nephrotic syndrome. 
Serum albumin degradation may occur in conditions such as fever, pregnancy poisoning defined as preeclampsia, thyroid disorders, and Cushing's disease. 
Apart from all these, pregnancy, excessive water consumption, use of certain drugs and heart failure, which trigger the increase in blood volume, also lead to a decrease in albumin levels.

Serum albumin has not traditionally been used as a routine preoperative test. 
There is no evidence for its use in a healthy population. However, the national VA surgical risk study showed that low serum albumin was a better predictor of surgical outcomes than many other preoperative patient characteristics when used in patients with comorbidities. 
The study showed that a decrease in serum albumin from 46 g/L to less than 21 g/L was associated with an increase in mortality from 1% to 29%. 
There was an increase in morbidity from 10% to 65%.

This test measures the amount of the protein albumin in your blood.

Your liver makes albumin. 
Albumin carries substances such as hormones, medicines, and enzymes throughout your body.

This test can help diagnose, evaluate, and watch kidney and liver conditions. 
When your kidneys start to fail, albumin starts to leak into your urine. 
This causes a low albumin level in your blood.

Human serum albumin (HSA) is the most abundant protein found in plasma and shows a typical blood concentration of 5 g/100 ml. 
Serum albumins physiological and pharmacological properties have been extensively studied over several decades . 
Such studies have revealed that HSA has a high affinity to a very wide range of materials, including metals such as Cu2+ and Zn2+, fatty acids, amino acids, metabolites such as bilirubin and for many drug compounds. 
The most important physiological role of the protein is therefore thought to be to bring such solutes in the bloodstream to their target organs, as well as to maintain the pH and osmotic pressure of plasma. 
In addition to its ordinary clinical applications, such as hypovolemic shock treatment, many investigators have attempted to utilize HSA as a carrier to deliver various drugs to their specific targets . 
The primary sequence of HSA shows that the protein is a single polypeptide with 585 residues containing 17 pairs of disulfide bridges and one free cysteine . 
Human serum albumin, as well as serum albumin from other species, has been found to consist of three homologous domains probably derived through gene multiplication (Brown, 1976). 
Despite many investigations using hydrodynamics, small-angle X-ray diffraction, electron microscopy and structural prediction, its three-dimensional molecular structure has remained largely unknown. 
Several crystal forms of HSA were reported in the 1970's , but they provided no structural information due to their poor reproducibility. 
The first crystal structure of HSA at low resolution was reported by Carter and co-workers in 1989 , and its refined structure at 2.8 Å resolution was published by the same group . 
The research group has also succeeded through extensive efforts in producing half a dozen different crystal forms of both HSA and non-human serum albumin, improving the resolution of their crystal structures and enhancing the knowledge of the diverse chemistry of serum albumin 
Recently, a couple of structures of HSA have been published by another research group , in which five myristates are accommodated in fatty acid sites. 
Not only did these studies shed light on the structural features of the protein, but knowledge of the three-dimensional structure also contributed to the clarification of how the protein binds various ligands. 
In this article, we describe a new crystal form of defatted HSA and discuss various molecular aspects of the protein as determined at the highest resolution so far reported.

Serum albumin is the most abundant protein in the blood plasma of mammals, reaching a concentration of 40 to 50 mg ml−1 in plasma, and it is the primary carrier of various solutes in plasma.
Serum albumins high abundance, stability and availability at high purity and low cost make serum albumin a model protein in many physicochemical and biomaterials science studies.
We have, in the past, elucidated the structural versatility and flexibility especially of human (and bovine) serum albumin through an electron paramagnetic resonance (EPR) spectroscopy-based research platform.

Concurrently, in the biomedical sciences there is an increasing need to develop new materials which simultaneously have the desired affinities to biological and therapeutic materials and high biocompatibility. 
Hydrogels made from synthetic or bio-macromolecules have exhibited great potential for biological and medical applications.
Among them, protein gels can be assumed to be cage-like unit structures forming a matrix in which the solvent (water in the case of hydrogels) and potentially releasable drugs and adjuvants are trapped.11

There has been an ongoing endeavor to synthesize hydrogels from serum albumin in such a way that robust, biocompatible hydrogels are delivered while preserving protein functionality, i.e. the capability to bind, retain, and release a variety of molecules in a well-defined manner. 
So far, very few (considering the abundance and availability of albumin) different synthetic methods have been developed and so far only hydrogels from bovine serum albumin (BSA), which has a primary sequence identity with human serum albumin (HSA) of ∼76%,16 have been reported. 
Here, we report, to the best of our knowledge for the first time, gels made from HSA (as well as from BSA, which have been described before), and we particularly focus on (i) systematically studying the conditions (temperature, pH and incubation time) under which gelation can take place, (ii) the characterization of the gels at the macroscopic level (mechanical properties as seen in rheological measurements) as well as (iii) the characterization of the accompanying changes in structure, dynamics, and functionality at the molecular level as seen in ATR-IR and electron paramagnetic resonance (EPR) spectroscopy.

Thermally induced BSA hydrogels are already well established and one finds long-standing work on the mechanism of thermally induced gelation of proteins such as BSA.17–19 Heating-induced gel formation consists of two sequential processes. 
First, unfolding of polypeptide segments induced by heating causes conformational changes and an altered tertiary structure in the protein. 
A subsequent phase of protein–protein (secondary structure element) interactions results in a progressive build-up of a network structure leading to the final gel.
The main disadvantage of this method is the extensive protein denaturation, with the risk of compromising protein functionality and biocompatibility.
The currently accepted working hypothesis states that in order to obtain thermally induced albumin hydrogels at neutral pH, the temperature must be set above the denaturation temperature of the protein (at pH 7.4 the denaturation temperature of serum albumin is 62 °C

Serum albumin is a carbohydrate-free protein, which constitutes 55% to 65% of total plasma protein. 
Serum albumin maintains oncotic plasma pressure, is involved in the transport and storage of a wide variety of ligands, and is a source of endogenous amino acids. 
Serum albumin binds and solubilizes various compounds, including bilirubin, calcium, long-chain fatty acids, toxic heavy metal ions, and numerous pharmaceuticals.

 
Hypoalbuminemia is caused by several factors: impaired synthesis due either to liver disease (primary) or due to diminished protein intake (secondary), increased catabolism as a result of tissue damage and inflammation, malabsorption of amino acids, and increased renal excretion

The types of proteins that must leak from blood vessels into body tissues cannot pass through relatively narrow spaces such as capillaries. 
Serum albumin provides the transportation of fatty acids, which are hardly water-soluble, to the tissues and organs through the blood, as well as the oncotic pressure it creates, allowing the passage of proteins that are large in size into narrow spaces.

The fluid balance between the veins and tissue spaces is ensured by the albumin that creates pressure in the vein. 
Thanks to albumin, which constitutes approximately 60% of the total protein amount in the blood, the accumulation of fluid in the tissues, that is, the formation of edema, is prevented.
Serum albumin, which is found in the fluids contained in the tissues, as well as in the blood plasma; It is a type of protein found in many regions such as sweat, tears, bile, gastric juice, muscle and skin.

Serum albumin, which provides the transport of nutrients and hormones in the blood to the relevant body parts, also plays a role in maintaining the acid-base balance of the body.

Serum albumin synthesized by the liver keeps these substances under control by binding to oxygen free radicals, also known as unstable atoms, which circulate freely in the body. 
Serum albumin neutralizes these metals by binding to the ions of minerals such as mercury, nickel, zinc and copper, which can be dangerous to the body.

Serum albumin; Vitamin B6 plays a role in the transport of drugs taken for treatment, thyroid and steroid hormones, as well as some fatty acids such as nitric acid (NO), oleic and linoleic.

Serum albumin binds to water-insoluble toxic wastes such as bilirubin (BIL), which is produced during the liver's breakdown of erythrocytes (red blood cells, red blood cells, RBC), and neutralizes such metabolic wastes.

Too little or too much albumin in the person's body can occur due to some diseases, as well as dehydration, excessive sweating, inadequate and unbalanced nutrition. 
Serum albumin reference values ​​(normal values) are 3.1 to 5.5 g/dL. 

IUPAC NAME:
-
SYNONYMS:

serum albumin.
ricin.
albumen.
lactalbumin.
simple protein.