| ¿µ¹® | protein | ÇÑ±Û | ´Ü¹éÁú |
|---|---|---|---|
| ¼³¸í | ź¼Ò, ¼ö¼Ò, »ê¼Ò, Áú¼Ò, ȲÀ» ÇÔÀ¯Çϰí ÀÖ´Â À¯±âÈÇÕ¹°·Î, ¸ðµç ¼¼Æ÷ÀÇ ¿øÇüÁúÀ» ÀÌ·ç°í ÀÖ´Â ±âº» ±¸¼º¹°ÁúÀÌ´Ù. ´Ü¹éÁúÀº ±× ´ÜÀ§ÀÎ ¾Æ¹Ì³ë»êµéÀÌ ÆéƼµå°áÇÕ¿¡ ÀÇÇØ °áÇյǾî ÀÖÀ¸¸ç, º¸Åë 20°³ÀÇ ¾Æ¹Ì³ë»êµéÀÌ ´Ù¸¥ ¼ø¼¿Í Á¶¼ºÀ» °¡Áö°í ¹è¿µÇ¾î, µ¶Æ¯ÇÑ ÇϳªÀÇ ´Ü¹éÁúÀ» Çü¼ºÇÏ°Ô µÈ´Ù. |
||
| Bmod | behavior modification |
|---|---|
| CM | California mastitis [test]; calmodulin; capreomycin; carboxymethyl; cardiac murmur; cardiac muscle; ... |
| CMS | children's medical services; Christian Medical Society; chronic myelodysplastic syndrome; chromosome... |
| EBM | electrophysiologic behavior modification; epidermal basement membrane; evidence-based medicine; expr... |
| ICD-9-CM | International Classification of Diseases-ninth revision-Clinical Modification |
| DMF | Dose modification factors |
|---|---|
| ICD9CM | International Classification of Diseases 9th Revision Clinical Modification |
| ICD-9 CM | International Classification of Diseases, Ninth Revision, Clinical Modification |
| MDRD | Modification of Diet in Renal Disease |
| R-M | Restriction and modification |
| modification | 1. A nonhereditary change in an organism; e.g., one that is acquired from its own activity or environment. 2. A chemical or structural alteration in a molecule. Behaviour modification, the systematic use of principles of conditioning and learning, especially operant or instrumental conditioning, to teach certain skills or to extinguish undesirable behaviours, attitudes, or phobias. Chemical modification, alteration in the structure of a molecule, typically a macromolecule such as a protein, by chemical means; often, the covalent addition by some reagent. Covalent modification, alteration in the structure of a macromolecule by enzymatic means, resulting in a change in the properties of that macromolecule; frequently, this type of modification is physiologically relevant. (05 Mar 2000) |
|---|---|
| modification enzyme | <enzyme, molecular biology> An enzyme that introduces minor bases into DNA or RNA or that alters bases already incorporated. Serves to alter the sequence so that restriction enzymes will not damage the strand. (18 Nov 1997) |
| post-translational modification | The enzymatic processing of a polypeptide chain after translation from messenger RNA and after peptide bond formation has occurred. Examples include glycosylation, acylation, limited proteolysis, phosphorylation, isoprenylation. (10 Oct 1997) |
| ScrFI modification methylase | <enzyme> From lactococcus lactis subsp. Cremoris uc503; recognises sequence ccngg and forms m(5)ccngg; see also DNA modification methylase dsav and DNA modification methylase ssoii Registry number: EC 2.1.1.- Synonym: scrfi methylase (26 Jun 1999) |
| host restriction-modification | A bacterial system where the bacterium is able to destroy invading DNA from a bacteriophage (virus which infects bacteria) while at the same time preventing the destruction of their own DNA. The phage DNA is cleaved by a restriction enzyme made by the bacterium, the bacterial DNA is modified (usually with methylation) so that the enzyme will not destroy it. (09 Oct 1997) |
| Stirling's modification of Gram's stain | <technique> A stable aniline-crystal violet stain. (05 Mar 2000) |
| DNA modification | <molecular biology> A variety of chemical changes made to a DNA molecule just after it has been replicated. An example is DNA methylation. (09 Oct 1997) |
| DNA modification methylases | <enzyme> Enzymes that are part of the restriction-modification systems. They are responsible for producing a species-characteristic methylation pattern, on either adenine or cytosine residues, in a specific short base sequence in the host cell's own DNA. This methylated sequence will occur many times in the hosT-cell DNA and remain intact for the lifetime of the cell. Any DNA from another species which gains entry into a living cell and lacks the characteristic methylation pattern will be recognised by the restriction endonucleases of similar specificity and destroyed by cleavage. most have been studied in bacterial systems, but a few have been found in eukaryotic organisms. Registry number: EC 2.1.1.- (12 Dec 1998) |
| DNA restriction-modification enzymes | Systems consisting of two enzymes, a modification methylase and a restriction endonuclease. They are closely related in their specificity and protect the DNA of a given bacterial species. The methylase adds methyl groups to adenine or cytosine residues in the same target sequence that constitutes the restriction enzyme binding site. The methylation renders the target site resistant to restriction, thereby protecting DNA against cleavage. (12 Dec 1998) |
| acetoacetyl-acyl carrier protein synthase | <enzyme> E coli enzyme, that catalyses condensation of malonyl-acyl carrier protein plus acetyl-acyl carrier protein; not inhibited by cerulenin Registry number: EC 2.3.1.- Synonym: acetoacetyl-acp synthase (26 Jun 1999) |
| acid soluble spore protein | <molecular biology> A DNA binding protein in the spores of some bacteria, thought to stabilise the DNA in an A configuration, so protecting it from cleavage by enzymes or UV light. (18 Nov 1997) |
| acute-phase protein | <haematology> These plasma proteins (in addition to fibrinogen) increase 25% or more in response to inflammation and injury are under direct control of interleukin-6 (IL-6) (hepatocyte-stimulating factor). Other proteins which increase are ceruloplasmin, C3 and C4 which increase 50% or more; alpha-1 acid glycoprotein, alpha-1 antitrypsin, haptoglobin and fibrinogen (the major determinant of viscosity 1 ) which increase two- to fourfold; C-reactive protein (CRP) and serum amyloid A which increase several hundred-fold. Despite long-held clinical opinion to the contrary, available data indicate that neither ESR nor measurement of specific acute-phase reactants are useful in excluding underlying infection or inflammation regardless of the pretest probability. These proteins are secreted into the blood in increased or decreased quantities by hepatocytes in response to trauma, inflammation, or disease. They can serve as inhibitors or mediators of the inflammatory processes. Certain acute-phase proteins have been used to diagnose and follow the course of diseases or as tumour markers. See also: amyloid, c-reactive protein, erythrocyte sedimentation rate, viscosity. (25 Jun 1999) |
| acyl-(acyl-carrier-protein)-phospholipid acyltransferase | <enzyme> Catalyses the formation of phosphatidylethanolamine from acyl-acyl carrier protein and 2-acyl-sn-glycero-3-phosphoethanolamine Registry number: EC 2.3.1.40 Synonym: 2-acyl-gpe acyltransferase, 2-acylglycerophosphoethanolamine acyltransferase (26 Jun 1999) |
| acyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine acyltransferase | <enzyme> E coli enzyme involved in lipid a biosynthesis; uses beta-hydroxymyristoyl-acyl carrier protein to form udp-3-monoacyl-n-acetylglucosamine; amino acid sequence given in second source Registry number: EC 2.3.1.129 Synonym: udp-aguatransferase, lpxa protein, udp-n-acetylglucosamine-3-acyltransferase, udp-n-acetylglucosamine 3-o-acyltransferase, udp-3-o-(r-3-hydroxymyristoyl)glucosamine-n-acyltransferase, lpxd protein, fira gene product, fira protein (26 Jun 1999) |
| acyl carrier protein | <protein> A small (77 peptides long) protein which binds six other enzymes involved in fatty acid synthesis. It was first isolated in E. Coli bacteria. (09 Oct 1997) |
Synonyms : Amino Acid Modification, Pre-Translational, Amino Acid Modification, Pretranslational, Amino Acid Modification, Translational, Co-Translational Amino Acid Modification, Co-Translational Protein Modification, Co-Translational Protein Processing
Á¦Ç°¸í |
ÆÇ¸Å»ç |
º¸ÇèÄÚµå | ¼ººÐ/ÇÔ·® | ±¸ºÐ/º¸Çè±Þ¿© |
|---|
Á¦Ç°¸í |
ÆÇ¸Å»ç |
º¸ÇèÄÚµå | ¼ººÐ/ÇÔ·® | ±¸ºÐ/º¸Çè±Þ¿© |
|---|