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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]
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 ...
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.
Structure of a typical L-alpha-amino acid in the "neutral" form. Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2]
Bovine serum albumin (BSA or "Fraction V") is a serum albumin protein derived from cows. It is often used as a protein concentration standard in lab experiments. The nickname "Fraction V" refers to albumin being the fifth fraction of the original Edwin Cohn purification methodology that made use of differential solubility characteristics of plasma proteins.
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.
The ovalbumin protein of chickens consists of 385 amino acids, its relative molecular mass is 42.7 kDa, [5] and it adopts a serpin-like structure. [6] Ovalbumin also has several modifications, including N-terminal acetylation (G1), phosphorylation (S68, S344), and glycosylation (N292). [5]
α-Lactalbumin is a source of amino acids which are connected to improved mental health. This protein is rich in tryptophan residues which are a precursor to serotonin, a neurotransmitter associated with positive moods. The protein also increases the plasma concentration for other large neutral amino acids (LNAAs) which help balance hormones.