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α-macroglobulin
Alpha globulins are a group of globular proteins in plasma that are highly mobile in alkaline or electrically charged solutions. They inhibit certain blood proteases and show significant inhibitor activity. The alpha globulins typically have molecular weights of around 93 kDa. Examples Alpha globulins include certain hormones, proteins that transport hormones, and other compounds, including prothrombin and HDL. Alpha 1 globulins * α1-antitrypsin * Alpha 1-antichymotrypsin *Orosomucoid (acid glycoprotein) * Serum amyloid A * Alpha 1-lipoprotein * Protein HC Alpha 2 globulins *Haptoglobin *Alpha-2u globulin * α2-macroglobulin *Ceruloplasmin *Thyroxine-binding globulin *Alpha 2-antiplasmin *Protein C *Alpha 2-lipoprotein *Angiotensinogen * Cortisol binding globulin *Vitamin D-binding protein Vitamin D-binding protein (DBP), also/originally known as gc-globulin (group-specific component), is a protein that in humans is encoded by the ''GC'' gene. DBP is genetically the oldes ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha 2-macroglobulin
α2-Macroglobulin (α2M) or alpha-2-macroglobulin is a large (720 KDa) plasma protein found in the blood. It is mainly produced by the liver, and also locally synthesized by macrophages, fibroblasts, and adrenocortical cells. In humans it is encoded by the ''A2M'' gene. α2-Macroglobulin acts as an antiprotease and is able to inactivate an enormous variety of proteinases. It functions as an inhibitor of fibrinolysis by inhibiting plasmin and kallikrein. It functions as an inhibitor of coagulation by inhibiting thrombin. α2-macroglobulin may act as a carrier protein because it also binds to numerous growth factors and cytokines, such as platelet-derived growth factor, basic fibroblast growth factor, TGF-β, insulin, and IL-1β. No specific deficiency with associated disease has been recognized, and no disease state is attributed to low concentrations of α2-macroglobulin. The concentration of α2-macroglobulin rises 10-fold or more in the nephrotic syndrome when other lower mo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Electrophoresis
Electrophoresis is the motion of charged dispersed particles or dissolved charged molecules relative to a fluid under the influence of a spatially uniform electric field. As a rule, these are zwitterions with a positive or negative net charge. Electrophoresis is used in laboratories to separate macromolecules based on their charges. The technique normally applies a negative charge called cathode so anionic protein molecules move towards a positive charge called anode. Therefore, electrophoresis of positively charged particles or molecules (cations) is sometimes called cataphoresis, while electrophoresis of negatively charged particles or molecules (anions) is sometimes called anaphoresis. Electrophoresis is the basis for analytical techniques used in biochemistry and molecular biology to separate particles, molecules, or ions by size, charge, or binding affinity, either freely or through a supportive medium using a one-directional flow of electrical charge. It is use ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha-1-microglobulin
Alpha-1-microglobulin (A1M, α1-microglobulin,B. Ekström, P.A. Peterson, I. Berggård "A urinary and plasma alpha-1-glycoprotein of low molecular weight: isolation and some properties." ''Biochem. Biophys. Res. Commun'' 1975, vol. sometimes also called Protein HC) is a microglobulin, a small globular protein. It is found in all vertebrates, including humans, and is distributed in blood plasma and extravascular tissues of all organs. It is synthesized in most cells of the body, but mainly in the liverAlpha-1-microglobulin: Innate defence against pathological oxidation by Magnus G Olsson, 2009 from a gene that codes for the alpha-1-microglobu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cortisol-binding Globulin
Transcortin, also known as corticosteroid-binding globulin (CBG) or serpin A6, is a protein produced in the liver in animals. In humans it is encoded by the SERPINA6 gene. It is an alpha-globulin. Function This gene encodes an alpha-globulin protein with corticosteroid-binding properties. This is the major transport protein for glucocorticoids and progestins in the blood of most vertebrates. The gene localizes to a chromosomal region containing several closely related serine protease inhibitors (serpins). Binding Transcortin binds several steroid hormones at high rates: * Cortisol - Approximately 90% of the cortisol in circulation is bound to transcortin. (The rest is bound to serum albumin.) Cortisol is thought to be biologically active only when it is not bound to transcortin. * Cortisone * Deoxycorticosterone (DOC) * Corticosterone - About 78% of serum corticosterone is bound to transcortin. * Aldosterone - Approximately 17% of serum aldosterone is bound to transcortin, whil ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Angiotensinogen
Angiotensin is a peptide hormone that causes vasoconstriction and an increase in blood pressure. It is part of the renin–angiotensin system, which regulates blood pressure. Angiotensin also stimulates the release of aldosterone from the adrenal cortex to promote sodium retention by the kidneys. An oligopeptide, angiotensin is a hormone and a dipsogen. It is derived from the precursor molecule angiotensinogen, a serum globulin produced in the liver. Angiotensin was isolated in the late 1930s (first named "angiotonin" or "hypertensin", later renamed "angiotensin" as a consensus by the 2 groups that independently discovered it) and subsequently characterized and synthesized by groups at the Cleveland Clinic and Ciba laboratories. Precursor and types Angiotensinogen Angiotensinogen is an α-2-globulin synthesized in the liver and is a precursor for angiotensin, but has also been indicated as having many other roles not related to angiotensin peptides. It is a member ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha 2-lipoprotein
A lipoprotein is a biochemical assembly whose primary function is to transport hydrophobic lipid (also known as fat) molecules in water, as in blood plasma or other extracellular fluids. They consist of a triglyceride and cholesterol center, surrounded by a phospholipid outer shell, with the hydrophilic portions oriented outward toward the surrounding water and lipophilic portions oriented inward toward the lipid center. A special kind of protein, called apolipoprotein, is embedded in the outer shell, both stabilising the complex and giving it a functional identity that determines its role. Plasma lipoprotein particles are commonly divided into five main classes, based on size, lipid composition, and apolipoprotein content. They are, in increasing size order: HDL, LDL, IDL, VLDL and chylomicrons. Subgroups of these plasma particles are primary drivers or modulators of atherosclerosis. Many enzymes, transporters, structural proteins, antigens, adhesins, and toxins are sometim ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein C
Protein C, also known as autoprothrombin IIA and blood coagulation factor XIV, is a zymogen, that is, an inactive enzyme. The activated form plays an important role in regulating anticoagulation, inflammation, and cell death and maintaining the permeability of blood vessel walls in humans and other animals. Activated protein C (APC) performs these operations primarily by proteolytically inactivating proteins Factor Va and Factor VIIIa. APC is classified as a serine protease since it contains a residue of serine in its active site. In humans, protein C is encoded by the ''PROC'' gene, which is found on chromosome 2. The zymogenic form of protein C is a vitamin K-dependent glycoprotein that circulates in blood plasma. Its structure is that of a two-chain polypeptide consisting of a light chain and a heavy chain connected by a disulfide bond. The protein C zymogen is activated when it binds to thrombin, another protein heavily involved in coagulation, and protein C' ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha 2-antiplasmin
Alpha 2-antiplasmin (or α2-antiplasmin or plasmin inhibitor) is a serine protease inhibitor (serpin) responsible for inactivating plasmin. Plasmin is an important enzyme that participates in fibrinolysis and degradation of various other proteins. This protein is encoded by the ''SERPINF2'' gene. Structure Alpha 2-antiplasmin (α2AP) is a member of the serine protease inhibitor (serpin) superfamily and is structurally characterized by a central serpin domain flanked by unique N-terminal, N- and C-terminal extensions. The mature human α2AP protein consists of 452 amino acids, with a 12-residue N-terminus, a central serpin domain, and a C-terminal tail of approximately 55 residues. The reactive center loop, which is crucial for its inhibitory function, protrudes from the central serpin domain and contains the Arg364-Met365 peptide bond that is specifically targeted and cleaved by plasmin. There are two main circulating form ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thyroxine-binding Globulin
Thyroxine-binding globulin (TBG) is a globulin protein encoded by the ''SERPINA7'' gene in humans. TBG binds thyroid hormones in circulation. It is one of three transport proteins (along with transthyretin and serum albumin) responsible for carrying the thyroid hormones thyroxine (T4) and triiodothyronine (T3) in the bloodstream. Of these three proteins, TBG has the highest affinity for T4 and T3 but is present in the lowest concentration relative to transthyretin and albumin, which also bind T3 and T4 in circulation. Despite its low concentration, TBG carries the majority of T4 in the blood plasma. Due to the very low concentration of T4 and T3 in the blood, TBG is rarely more than 25% saturated with its ligand. Unlike transthyretin and albumin, TBG has a single binding site for T4/T3. TBG is synthesized primarily in the liver as a 54- kDa protein. In terms of genomics, TBG is a serpin Serpins are a superfamily of proteins with similar structures that were first id ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ceruloplasmin
Ceruloplasmin (or caeruloplasmin) is a ferroxidase enzyme that in humans is encoded by the ''CP'' gene. Ceruloplasmin is the major copper-carrying protein in the blood, and in addition plays a role in iron metabolism. It was first described in 1948. Another protein, hephaestin, is noted for its homology to ceruloplasmin, and also participates in iron and probably copper metabolism. Function Ceruloplasmin (CP) is an enzyme () synthesized in the liver containing 6 atoms of copper in its structure. Ceruloplasmin carries more than 95% of the total copper in healthy human plasma. The rest is accounted for by macroglobulins. Ceruloplasmin exhibits a copper-dependent oxidase activity, which is associated with possible oxidation of Fe2+ (ferrous iron) into Fe3+ (ferric iron), therefore assisting in its transport in the plasma in association with transferrin, which can carry iron only in the ferric state. The molecular weight of human ceruloplasmin is reported to be 151kDa. Despit ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha-2u Globulin
Major urinary proteins (Mups), also known as α2u-globulins, are a subfamily of proteins found in abundance in the urine and other secretions of many animals. Mups provide a small range of identifying information about the donor animal, when detected by the vomeronasal organ of the receiving animal. They belong to a larger family of proteins known as lipocalins. Mups are encoded by a cluster of genes, located adjacent to each other on a single stretch of DNA, that varies greatly in number between species: from at least 21 functional genes in mice to none in humans. Mup proteins form a characteristic glove shape, encompassing a ligand-binding pocket that accommodates specific small organic chemicals. Urinary proteins were first reported in rodents in 1932, during studies by Thomas Addis into the cause of proteinuria. They are potent human allergens and are largely responsible for a number of animal allergies, including to cats, horses and rodents. Their endogenous function with ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Haptoglobin
Haptoglobin (abbreviated as Hp) is the protein that in humans is encoded by the ''HP'' gene. In blood plasma, haptoglobin binds with high affinity to ''free'' hemoglobin released from erythrocytes, and thereby inhibits its deleterious oxidative activity. Compared to Hp, hemopexin binds to ''free'' heme. The haptoglobin-hemoglobin complex will then be removed by the reticuloendothelial system (mostly the spleen). In clinical settings, the haptoglobin assay is used to screen for and monitor intravascular hemolytic anemia. In intravascular hemolysis, free hemoglobin will be released into circulation and hence haptoglobin will bind the hemoglobin. This causes a decline in haptoglobin levels. The protein was discovered as a "plasma substance" in 1938 by French biochemists Max-Fernand Jayle and Michel Polonovski. Function Hemoglobin that has been released into the blood plasma by damaged red blood cells has harmful effects. The ''HP'' gene encodes a preproprotein that is proc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
