Serum albumin

1AO6, 1BJ5, 1BKE, 1BM0, 1E78, 1E7A, 1E7B, 1E7C, 1E7E, 1E7F, 1E7G, 1E7H, 1E7I, 1GNI, 1GNJ, 1H9Z, 1HA2, 1HK1, 1HK2, 1HK3, 1HK4, 1HK5, 1N5U, 1O9X, 1TF0, 1UOR, 1YSX, 2BX8, 2BXA, 2BXB, 2BXC, 2BXD, 2BXF, 2BXG, 2BXH, 2BXI, 2BXK, 2BXL, 2BXM, 2BXN, 2BXO, 2BXP, 2BXQ, 2I2Z, 2I30, 2VDB, 2VUE, 2VUF, 2XSI, 2XVQ, 2XVU, 2XVV, 2XVW, 2XW0, 2XW1, 2YDF, 3A73, 3B9L, 3B9M, 3CX9, 3JQZ, 3JRY, 3LU6, 3LU7, 3LU8, 3SQJ, 3TDL, 3UIV, 4E99, 4EMX, 4G03, 4G04, 4HGK, 4HGM, 4IW1, 4IW2, 4K2C, 4L8U, 4L9K, 4L9Q, 4LA0, 4LB9, 4LB2, 2N0X, 2ESG, 4S1Y, 4N0F, 4Z69, 4N0U, 4K71, 2BXE, 4BKE, 5IJF, 5ID7, 5IFO, 5FUO21311657ENSG00000163631ENSMUSG00000029368P02768P07724NM_000477NM_009654NP_000468NP_033784Serum 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.1ao6: CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN1bj5: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID1bke: HUMAN SERUM ALBUMIN IN A COMPLEX WITH MYRISTIC ACID AND TRI-IODOBENZOIC ACID1bm0: CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN1e78: CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN1e7a: CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN COMPLEXED WITH THE GENERAL ANESTHETIC PROPOFOL1e7b: CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN COMPLEXED WITH THE GENERAL ANESTHETIC HALOTHANE1e7c: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID AND THE GENERAL ANESTHETIC HALOTHANE1e7e: HUMAN SERUM ALBUMIN COMPLEXED WITH DECANOIC ACID (CAPRIC ACID)1e7f: HUMAN SERUM ALBUMIN COMPLEXED WITH DODECANOIC ACID (LAURIC ACID)1e7g: HUMAN SERUM ALBUMIN COMPLEXED WITH TETRADECANOIC ACID (MYRISTIC ACID) HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID1e7h: HUMAN SERUM ALBUMIN COMPLEXED WITH HEXADECANOIC ACID (PALMITIC ACID)1e7i: HUMAN SERUM ALBUMIN COMPLEXED WITH OCTADECANOIC ACID (STEARIC ACID)1gni: HUMAN SERUM ALBUMIN COMPLEXED WITH CIS-9-OCTADECENOIC ACID (OLEIC ACID)1gnj: HUMAN SERUM ALBUMIN COMPLEXED WITH CIS-5,8,11,14-EICOSATETRAENOIC ACID (ARACHIDONIC ACID)1h9z: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID AND THE R-(+) ENANTIOMER OF WARFARIN1ha2: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID AND THE S-(-) ENANTIOMER OF WARFARIN1hk1: HUMAN SERUM ALBUMIN COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE)1hk2: HUMAN SERUM ALBUMIN MUTANT R218H COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE)1hk3: HUMAN SERUM ALBUMIN MUTANT R218P COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE)1hk4: HUMAN SERUM ALBUMIN COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE) AND MYRISTIC ACID (TETRADECANOIC ACID)1hk5: HUMAN SERUM ALBUMIN MUTANT R218H COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE) AND MYRISTIC ACID (TETRADECANOIC ACID)1n5u: X-RAY STUDY OF HUMAN SERUM ALBUMIN COMPLEXED WITH HEME1o9x: HUMAN SERUM ALBUMIN COMPLEXED WITH TETRADECANOIC ACID (MYRISTIC ACID) AND HEMIN1tf0: Crystal structure of the GA module complexed with human serum albumin1uor: X-RAY STUDY OF RECOMBINANT HUMAN SERUM ALBUMIN. PHASES DETERMINED BY MOLECULAR REPLACEMENT METHOD, USING LOW RESOLUTION STRUCTURE MODEL OF TETRAGONAL FORM OF HUMAN SERUM ALBUMIN1ysx: Solution structure of domain 3 from human serum albumin complexed to an anti-apoptotic ligand directed against Bcl-xL and Bcl-22bx8: HUMAN SERUM ALBUMIN COMPLEXED WITH AZAPROPAZONE2bxa: HUMAN SERUM ALBUMIN COMPLEXED WITH 3-CARBOXY-4-METHYL-5-PROPYL-2-FURANPROPANOIC ACID (CMPF)2bxb: HUMAN SERUM ALBUMIN COMPLEXED WITH OXYPHENBUTAZONE2bxc: HUMAN SERUM ALBUMIN COMPLEXED WITH PHENYLBUTAZONE2bxd: HUMAN SERUM ALBUMIN COMPLEXED WITH WARFARIN2bxe: HUMAN SERUM ALBUMIN COMPLEXED WITH DIFLUNISAL2bxf: HUMAN SERUM ALBUMIN COMPLEXED WITH DIAZEPAM2bxg: HUMAN SERUM ALBUMIN COMPLEXED WITH IBUPROFEN2bxh: HUMAN SERUM ALBUMIN COMPLEXED WITH INDOXYL SULFATE2bxi: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND AZAPROPAZONE2bxk: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE, AZAPROPAZONE AND INDOMETHACIN2bxl: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND 3,5-DIIODOSALICYLIC ACID2bxm: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND INDOMETHACIN2bxn: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND IODIPAMIDE2bxo: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND OXYPHENBUTAZONE2bxp: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND PHENYLBUTAZONE2bxq: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE, PHENYLBUTAZONE AND INDOMETHACIN2i2z: Human serum albumin complexed with myristate and aspirin2i30: Human serum albumin complexed with myristate and salicylic acid 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. 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. It 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. 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). 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. 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. Albumin is a globular, water-soluble, un-glycosylated serum protein of approximate molecular weight of 65,000 Daltons. 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. The general structure of albumin is characterized by several long α helices allowing it to maintain a relatively static shape, which is essential for regulating blood pressure. Serum albumin contains eleven distinct binding domains for hydrophobic compounds. One hemin and six long-chain fatty acids can bind to serum albumin at the same time.