| E* | lesion on the erythrocyte cell membrane at the site of complement fixation |
|---|---|
| FMR | fragile site mental retardation [syndrome]; Friend-Moloney-Rauscher [antigen] |
| fra | fragil [site] |
| FRAXE | X-linked mental retardation-fragile site [syndrome] |
| HBVS | hepatitis B virus integration site |
| binding energy | <chemistry, radiobiology> The binding energy of a nucleus is the minimum energy required to dissociate it into its component neutrons and protons. Neutron or proton binding energies are those required to remove a neutron or proton, respectively, from a nucleus. Electron binding energy is that required to remove an electron from an atom or a molecule. (16 Dec 1997) |
|---|---|
| calcium-binding protein | <biochemistry> There are two main groups of calcium binding proteins, those that are similar to calmodulin and are called EF hand proteins and those that bind calcium and phospholipid (e.g. Lipocortin) and that have been grouped under the generic name of annexins. Many other proteins will bind calcium, although the binding site usually has considerable homology with the calcium-binding domains of calmodulin. They can act as transport proteins, regulator proteins or activator proteins. There is also a vitamin D-dependent variant which is a protein that plays a fundamental role in the vitamin d mediated transport of calcium in reptiles, amphibians, birds and mammals. It is found in the intestine, kidneys, egg shell gland, brain, and possibly other organs. Its molecular weight is species dependent. (12 May 2002) |
| calmodulin-binding proteins | Proteins which bind calmodulin. They are found in many tissues and have a variety of functions including f-actin cross-linking properties, inhibition of cyclic nucleotide phosphodiesterase and calcium and magnesium atpases. (12 Dec 1998) |
| cap binding protein | <molecular biology, protein> Protein (24 kD) with affinity for cap structure at 5' end of mRNA that probably assists, together with other initiation factors, in binding the mRNA to the 40S ribosomal subunit. Translation of mRNA in vitro is faster if it has a cap binding protein. (18 Nov 1997) |
| galactose binding protein | <protein> A bacterial periplasmic protein, most studied in E. Coli, that acts both as a sensory element in the detection of galactose as a chemotactic signal and in the uptake of the sugar. (18 Nov 1997) |
| Raji cell binding test | <investigation> A test for the detection of soluble IgG antigen complexes. Raji cells are a line of EBV transformed lymphocytes with surface Fc receptors. Complexes are detected by their ability to compete with a radiolabelled aggregated IgG for binding to the cells. (18 Nov 1997) |
| maltose binding protein | <protein> Protein of the bacterial (E. Coli) surface that links with MCP II and is involved in the chemotactic response to maltose, probably derived from a similar protein that links with a trans membrane transport system. (18 Nov 1997) |
| vitamin d-binding protein | An alpha-globulin found in the plasma of man and other vertebrates. It is apparently synthesised in the liver and carries vitamin d and its metabolites through the circulation and mediates the response of tissue. It is also known as group-specific component (gc). Gc subtypes are used to determine specific phenotypes and gene frequencies. These data are employed in the classification of population groups, paternity investigations, and in forensic medicine. (12 Dec 1998) |
| cellular retinoic acid binding protein | <protein> A cytoplasmic fatty acid binding protein that acts as an initial receptor for the putative morphogen, retinoic acid. (18 Nov 1997) |
| retinol-binding protein | <molecular biology> Proteins which bind with retinol. The retinol-binding protein found in plasma has an alpha-1 mobility on electrophoresis and a molecular weight of 21,000-22,000. The protein has one binding site for retinol and is responsible for the transport of vitamin A. The retinol- protein complex (molecular weight 80,000 to 90,000) circulates in plasma in the form of a protein-protein complex with prealbumin. The retinol-binding protein found in tissue has a molecular weight of 14,000 and carries retinol as a non-covalently-bound ligand. (03 Jul 1999) |
| gonadal steroid-binding globulin | A protein that transports 65% of the testosterone in plasma. Synonym: sex steroid-binding globulin. (05 Mar 2000) |
| periplasmic binding proteins | Transport proteins located within the periplasmic space. Some act as receptors for bacterial chemotaxis, interacting with MCPs. Their mode of action is unclear. (18 Nov 1997) |
| ribose binding protein | <protein> Periplasmic binding proteins of bacteria that interact either with the ribose transport system or with the methyl accepting chemotaxis protein MCP III (trg). (18 Nov 1997) |
| GTP-binding protein | <molecular biology, protein> There are two main classes of G-proteins, the heterotrimeric G proteins that associate with receptors of the seven transmembrane domain superfamily and are involved in signal transduction and the small cytoplasmic G-proteins. Regulatory proteins found in all cells. They are versatile molecular switches, involved in the control of a wide range of biological processes - protein synthesis, signal transduction pathways, growth and differentiation. They all act through a common molecular mechanism based on their ability to bind the guanine nucleotides GTP and GDP selectively and with high affinity. Stimulatory G-proteins are permanently activated by cholera toxin, inhibitory ones by pertussis toxin. Transducin was one of the first of the heterotrimeric G-proteins to be identified. The small G-proteins are a diverse group of monomeric GTPases that include ras, rab, rac and rho and that play an important part in regulating many intracellular processes including cytoskeletal organisation and secretion. Their GTPase activity is regulated by activators (GAPs) and inhibitors (GIPs) that determine the duration of the active state. (12 Jul 2000) |
| RNA-binding proteins | Proteins which bind to RNA molecules. Certain structure motifs are common to several of the proteins, such as arginine (arg)-rich tracts, typically consisting of alternating arg-asp, arg-ser, or arg-gly residues. These proteins also tend to have a common ribonucleotide sequence domain. (12 Dec 1998) |