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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]
When two, highly protein-bound drugs (A and B) are added into the same biological system it will lead to an initial small increase in the concentration of free drug A (as drug B ejects some of the drug A from its proteins). However, this free drug A is now more available for redistribution into the body tissues and/or for excretion.
Serum albumin accounts for 55% of blood proteins, [1] is a major contributor to maintaining the oncotic pressure of plasma and assists, as a carrier, in the transport of lipids and steroid hormones. Globulins make up 38% of blood proteins and transport ions, hormones, and lipids assisting in immune function.
Oncotic pressure strongly affects the physiological function of the circulatory system. It is suspected to have a major effect on the pressure across the glomerular filter. However, this concept has been strongly criticised and attention has shifted to the impact of the intravascular glycocalyx layer as the major player. [2] [3] [4] [5]
The plasma total calcium concentration is in the range of 2.2–2.6 mmol/L (9–10.5 mg/dL), and the normal ionized calcium is 1.3–1.5 mmol/L (4.5–5.6 mg/dL). [4] The amount of total calcium in the blood varies with the level of plasma albumin, the most abundant protein in plasma, and therefore the main carrier of protein-bound calcium in the blood.
The Cohn process, developed by Edwin J. Cohn, is a series of purification steps with the purpose of extracting albumin from blood plasma.The process is based on the differential solubility of albumin and other plasma proteins based on pH, ethanol concentration, temperature, ionic strength, and protein concentration.
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 ...