| D007328 |
Insulin |
A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1). |
Iletin,Insulin A Chain,Insulin B Chain,Insulin, Regular,Novolin,Sodium Insulin,Soluble Insulin,Chain, Insulin B,Insulin, Sodium,Insulin, Soluble,Regular Insulin |
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| D007770 |
L-Lactate Dehydrogenase |
A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist. |
Lactate Dehydrogenase,Dehydrogenase, L-Lactate,Dehydrogenase, Lactate,L Lactate Dehydrogenase |
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| D008970 |
Molecular Weight |
The sum of the weight of all the atoms in a molecule. |
Molecular Weights,Weight, Molecular,Weights, Molecular |
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| D009211 |
Myoglobin |
A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group. |
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| D010047 |
Ovalbumin |
An albumin obtained from the white of eggs. It is a member of the serpin superfamily. |
Serpin B14 |
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| D010434 |
Pepsin A |
Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice. |
Pepsin,Pepsin 1,Pepsin 3 |
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| D011506 |
Proteins |
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. |
Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene |
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| D002621 |
Chemistry |
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange. |
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| D002919 |
Chymotrypsinogen |
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Alpha-Chymotrypsinogen,Chymotrypsinogen A,Chymotrypsinogen beta,Alpha Chymotrypsinogen,beta, Chymotrypsinogen |
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| D003580 |
Cytochromes |
Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands. |
Cytochrome |
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