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11657 Ensembl ENSG00000163631 ENSMUSG00000029368 UniProt P02768 P07724 RefSeq (mRNA) NM_000477 NM_009654 RefSeq (protein) NP_000468 NP_033784 Location (UCSC) Chr 4: 73.4 – 73.42 Mb Chr 5: 90.61 – 90.62 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Human serum albumin is the serum albumin found in human blood. It is the most abundant protein in human blood plasma ; it ...
The 3D structure of human serum albumin has been determined by X-ray crystallography to a resolution of 2.5 ångströms (250 pm). [1] Albumin is a 65–70 kDa protein. Albumin comprises three homologous domains that assemble to form a heart-shaped protein. [2] Each domain is a product of two subdomains that possess common structural motifs. [2]
The serum-ascites albumin gradient or gap (SAAG) is a calculation used in medicine to help determine the cause of ascites. [1] The SAAG may be a better discriminant than the older method of classifying ascites fluid as a transudate versus exudate. [2] The formula is as follows: SAAG = (serum albumin) − (albumin level of ascitic fluid).
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 . [ 2 ] [ 3 ] [ 4 ] Other mammalian forms, such as bovine serum albumin , are chemically similar.
Since albumin is alkalotic, acidic and neutral drugs will primarily bind to albumin. If albumin becomes saturated, then these drugs will bind to lipoprotein. Basic drugs will bind to the acidic alpha-1 acid glycoprotein. This is significant because various medical conditions may affect the levels of albumin, alpha-1 acid glycoprotein, and ...
Electrophoresis is a laboratory technique in which the blood serum (the fluid portion of the blood after the blood has clotted) is applied to either an acetate membrane soaked in a liquid buffer, [3] or to a buffered agarose gel matrix, or into liquid in a capillary tube, and exposed to an electric current to separate the serum protein ...
This method is significantly simplified compared to the Cohn Process. Its goal is to create high albumin yields as long as albumin is the sole product. Through a two-stage process, impurities are precipitated directly from fractions II and III supernatant at 42% ethanol, pH 5.8, temperature −5 degrees C, 1.2% protein, and 0.09 ionic strength.
Albumin is commonly used to replenish and maintain blood volume after traumatic injury, during surgery, and during plasma exchange. [3] Since albumin is the most abundant protein in the plasma its use may be the most well known, but many other proteins, although present in low concentrations, can have important clinical uses. [ 1 ]
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