| ¿µ¹® | serum proteins | ÇÑ±Û | Ç÷û´Ü¹é |
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||
| PBPs | Penicillin-Binding Proteins |
|---|---|
| GTP | Guanosine Tri-Phosphate |
| GTP | glutamyl transpeptidase; guanosine triphosphate |
| ABP | actin-binding protein; ambulatory blood pressure; American Board of Pedodontics; American Board of P... |
| CBP | calcium-binding protein; carbohydrate-binding protein; cardiopulmonary bypass; chlorobiphenyl; cobal... |
| G-proteins | GTP)-binding regulatory proteins |
|---|---|
| GTP-CH | GTP cyclohydrolase I |
| G proteins | GIP-binding proteins |
| G-proteins | Guanine nucleotide-binding regulatory proteins |
| G proteins | reglatory proteins |
| 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) |
|---|---|
| androgen-binding proteins | Carrier proteins produced in the sertoli cells of the testis, secreted into the seminiferous tubules, and transported via the efferent ducts to the epididymis. Participate in the transport of androgens; include also synthetic androgens binding proteins. (12 Dec 1998) |
| 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) |
| 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) |
| 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) |
| DNA-binding proteins | Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases. (12 Dec 1998) |
| insulin-like growth-factor-binding proteins | A family of soluble proteins that bind insulin-like growth factors and modulate their biological actions at the cellular level. (int j gynaecol obstet 1992;39(1):3-9) (12 Dec 1998) |
| thyroxine-binding proteins | A group of proteins that includes thyroxine-binding globulin, a glycoprotein that serves as the major and specific carrier of thyroxine in plasma, accounting for 70-75% of the bound thyroxine; thyroxine-binding prealbumin, an albumin that serves as the secondary carrier, accounting for between 20 and 25% of the bound thyroxine; and serum albumin, which accounts for the remaining bound thyroxine. (12 Dec 1998) |
| fatty acid binding proteins | <biochemistry> Group of small cytosolic proteins that bind fatty acids or other organic solutes. (18 Nov 1997) |
| GTP | An immediate precursor of guanine nucleotides in RNA; similar to ATP; has a crucial role in microtubule formation. GTP cyclohydrolase, an enzyme that catalyses the reaction of GTP and H2O forming formate and a precursor of tetrahydrobiopterin; a deficiency of this enzyme will result in one form of malignant hyperphenylalaninaemia. Acronym: GTP (05 Mar 2000) |
| GTP cyclohydrolase | <enzyme> (GTP cyclohydrolase I) or GTP 7,8-8,9-dihydrolase (pyrophosphate-forming) (GTP cyclohydrolase II). An enzyme group that hydrolyzes the imidazole ring of GTP, releasing carbon-8 as formate. Two c-n bonds are hydrolyzed and the pentase unit is isomerised. This is the first step in the synthesis of folic acid from GTP.6 (GTP cyclohydrolase I) and GTP cyclohydrolase II. Chemical name: GTP 7,8-8,9-dihydrolase Registry number: EC 3.5.4.16 (12 Dec 1998) |
| GTP phosphohydrolase | <enzyme> An enzyme that hydrolyzes GTP to GDP and provides energy for peptide chain elongation. Registry number: EC 3.6.1.- (12 Dec 1998) |
| GTP pyrophosphokinase | <enzyme> An enzyme that catalyses reversibly the transfer of a pyrophosphate group from ATP to the 3'-oh group of GDP or GTP with the formation of guanosine 3'-diphosphate 5'-diphosphate or guanosine 3'-diphosphate 5'-triphosphate and AMP. The enzyme, also called stringent factor, is located in the rela gene in stringent strains of bacteria. The above synthesis is induced by mRNA and uncharged trna which is bound to the aminoacyl-t-RNA binding site of the ribosome by a codon-specific association. Chemical name: ATP:GTP 3'-pyrophosphotransferase Registry number: EC 2.7.6.5 (12 Dec 1998) |
| GTP-RNA guanylyltransferase | <enzyme> Catalyses addition of GMP residue to 3'-ends of oligonucleotide primers Registry number: EC 2.7.7.- Synonym: terminal guanylyltransferase (26 Jun 1999) |
| phosphoenolpyruvate carboxykinase (GTP) | <enzyme> An enzyme of the lyase class that catalyses the conversion of GTP and oxaloacetate to GDP, phosphoenolpyruvate, and carbon dioxide. This reaction is part of gluconeogenesis in the liver. The enzyme occurs in both the mitochondria and cytosol of mammalian liver. Chemical name: GTP:oxaloacetate carboxy-lyase (transphosphorylating) Registry number: EC 4.1.1.32 (12 Dec 1998) |
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