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Index Alpha-2-Macroglobulin

alpha-2-Macroglobulin (α2M) is a large (720 KDa) plasma protein found in the blood. [1]

47 relations: Active site, Alzheimer's disease, Amine, Amino acid, Amyloid, Aspartic protease, Blood, Blood proteins, Bond cleavage, Catalysis, Chronic kidney disease, Coagulation, Conformational change, Conserved sequence, Copper, Cysteine protease, Enzyme inhibitor, Ester, Fibrinolysis, Fibroblast, Homo sapiens, Kallikrein, Kidney, Liver, Macrophage, MEROPS, Metalloproteinase, Molecular binding, Nephrotic syndrome, Oncotic pressure, Plasmin, Polymorphism (biology), Protease, Protease inhibitor (biology), Protein, Protein complex, Protein family, Protein structure, Proteolysis, Receptor (biochemistry), Serine protease, Steric effects, Substrate (chemistry), Tetrameric protein, Thiol, Thrombin, Zinc.

Active site

In biology, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction.

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Alzheimer's disease

Alzheimer's disease (AD), also referred to simply as Alzheimer's, is a chronic neurodegenerative disease that usually starts slowly and worsens over time.

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In organic chemistry, amines are compounds and functional groups that contain a basic nitrogen atom with a lone pair.

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Amino acid

Amino acids are organic compounds containing amine (-NH2) and carboxyl (-COOH) functional groups, along with a side chain (R group) specific to each amino acid.

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Amyloids are aggregates of proteins that become folded into a shape that allows many copies of that protein to stick together forming fibrils.

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Aspartic protease

Aspartic proteases are a catalytic type of protease enzymes that use an activated water molecule bound to one or more aspartate residues for catalysis of their peptide substrates.

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Blood is a body fluid in humans and other animals that delivers necessary substances such as nutrients and oxygen to the cells and transports metabolic waste products away from those same cells.

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Blood proteins

Blood proteins, also termed plasma proteins, are proteins present in blood plasma.

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Bond cleavage

Bond cleavage, or scission, is the splitting of chemical bonds.

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Catalysis is the increase in the rate of a chemical reaction due to the participation of an additional substance called a catalysthttp://goldbook.iupac.org/C00876.html, which is not consumed in the catalyzed reaction and can continue to act repeatedly.

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Chronic kidney disease

Chronic kidney disease (CKD) is a type of kidney disease in which there is gradual loss of kidney function over a period of months or years.

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Coagulation (also known as clotting) is the process by which blood changes from a liquid to a gel, forming a blood clot.

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Conformational change

In biochemistry, a conformational change is a change in the shape of a macromolecule, often induced by environmental factors.

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Conserved sequence

In evolutionary biology, conserved sequences are similar or identical sequences in nucleic acids (DNA and RNA) or proteins across species (orthologous sequences) or within a genome (paralogous sequences).

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Copper is a chemical element with symbol Cu (from cuprum) and atomic number 29.

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Cysteine protease

Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins.

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Enzyme inhibitor

4QI9) An enzyme inhibitor is a molecule that binds to an enzyme and decreases its activity.

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In chemistry, an ester is a chemical compound derived from an acid (organic or inorganic) in which at least one –OH (hydroxyl) group is replaced by an –O–alkyl (alkoxy) group.

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Fibrinolysis is a process that prevents blood clots from growing and becoming problematic.

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A fibroblast is a type of biological cell that synthesizes the extracellular matrix and collagen, the structural framework (stroma) for animal tissues, and plays a critical role in wound healing.

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Homo sapiens

Homo sapiens is the systematic name used in taxonomy (also known as binomial nomenclature) for the only extant human species.

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Kallikreins are a subgroup of serine proteases, enzymes capable of cleaving peptide bonds in proteins.

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The kidneys are two bean-shaped organs present in left and right sides of the body in vertebrates.

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The liver, an organ only found in vertebrates, detoxifies various metabolites, synthesizes proteins, and produces biochemicals necessary for digestion.

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Macrophages (big eaters, from Greek μακρός (makrós).

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MEROPS is an on-line database for peptidases (also known as proteases, proteinases and proteolytic enzymes) and their inhibitors.

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A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal.

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Molecular binding

Molecular binding is an attractive interaction between two molecules that results in a stable association in which the molecules are in close proximity to each other.

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Nephrotic syndrome

Nephrotic syndrome is a collection of symptoms due to kidney damage.

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Oncotic pressure

Oncotic pressure, or colloid osmotic pressure, is a form of osmotic pressure exerted by proteins, notably albumin, in a blood vessel's plasma (blood/liquid) that usually tends to pull water into the circulatory system.

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Plasmin is an important enzyme present in blood that degrades many blood plasma proteins, including fibrin clots.

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Polymorphism (biology)

Polymorphism in biology and zoology is the occurrence of two or more clearly different morphs or forms, also referred to as alternative phenotypes, in the population of a species.

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A protease (also called a peptidase or proteinase) is an enzyme that performs proteolysis: protein catabolism by hydrolysis of peptide bonds.

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Protease inhibitor (biology)

In biology and biochemistry, protease inhibitors are molecules that inhibit the function of proteases (enzymes that aid the breakdown of proteins).

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Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues.

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Protein complex

A protein complex or multiprotein complex is a group of two or more associated polypeptide chains.

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Protein family

A protein family is a group of evolutionarily-related proteins.

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Protein structure

Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule.

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Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids.

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Receptor (biochemistry)

In biochemistry and pharmacology, a receptor is a protein molecule that receives chemical signals from outside a cell.

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Serine protease

Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the (enzyme's) active site.

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Steric effects

Steric effects are nonbonding interactions that influence the shape (conformation) and reactivity of ions and molecules.

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Substrate (chemistry)

In chemistry, a substrate is typically the chemical species being observed in a chemical reaction, which reacts with a reagent to generate a product.

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Tetrameric protein

A tetrameric protein is a protein with a quaternary structure of four subunits (tetrameric).

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Thiol is an organosulfur compound that contains a carbon-bonded sulfhydryl (R–SH) group (where R represents an alkyl or other organic substituent).

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Thrombin (fibrinogenase, thrombase, thrombofort, topical, thrombin-C, tropostasin, activated blood-coagulation factor II, blood-coagulation factor IIa, factor IIa, E thrombin, beta-thrombin, gamma-thrombin) is a serine protease, an enzyme that, in humans, is encoded by the F2 gene.

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Zinc is a chemical element with symbol Zn and atomic number 30.

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A2-Macroglobulin, Alpha 2-macroglobulin, Alpha-2 macroglobulin, Alpha-2-macroglobulin, Alpha-macroglobulin, Alpha-macroglobulins, Alpha2-Macroglobulin, Alpha2-macroglobulin, Α2-macroglobulin.


[1] https://en.wikipedia.org/wiki/Alpha-2-Macroglobulin

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