| ¿µ¹® | Dilatation and Curettage(D & C) | ÇÑ±Û | Àڱñܾ¼ú, ÀڱøñÈ®Àå |
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| RE | radium emanation; readmission; rectal examination; reference emitter; reflux esophagitis; regional e... |
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| RFLPs | Restriction Fragment Length Polymorphisms; Á¦ÇÑÈ¿¼Ò´ÜÆíÀå´ÙÇü |
| FR | failure rate; film-screen radiograph; fasciculus retroflexus; febrile reaction; feedback regulation;... |
| RELP | restriction fragment length polymorphism |
| RELV | restriction fragment length variant |
| R-M | Restriction and modification |
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| RM | Restriction 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 |
acute angle
| 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) |
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| 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) |
| 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) |
| 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) |
| cell cycle restriction point | <cell biology, molecular biology> A point, late in G1, after which the cell must, normally, proceed through to division at its standard rate. (26 Mar 1998) |
| restriction | 1. The process with which foreign DNA that has been introduced into a prokaryotic cell becomes ineffective. 2. A limitation. (05 Mar 2000) |
| restriction endonuclease | <enzyme, molecular biology> Class of bacterial enzymes that cut DNA at specific sites. In bacteria their function is to destroy foreign DNA, such as that of bacteriophages (host DNA is specifically modified at these sites). Type I restriction endonucleases occur as a complex with the methylase and a polypeptide that binds to the recognition site on DNA. They are often not very specific and cut at a remote site. Type II restriction endonucleases are the classic experimental tools. They have very specific recognition and cutting sites. The recognition sites are short, 4-8 nucleotides and are usually palindromic sequences. Because both strands have the same sequence running in opposite directions the enzymes make double stranded breaks, which, if the site of cleavage is off centre, generates fragments with short single stranded tails, these can hybridise to the tails of other fragments and are called sticky ends. They are generally named according to the bacterium from which they were isolated (first letter of genus name and the first two letters of the specific name). The bacterial strain is identified next and multiple enzymes are given Roman numerals. For example the two enzymes isolated from the R strain of E. Coli are designated Eco RI and Eco RII. (10 Mar 1998) |
| restriction enzyme | <enzyme, molecular biology> Class of bacterial enzymes that cut DNA at specific sites. In bacteria their function is to destroy foreign DNA, such as that of bacteriophages (host DNA is specifically modified at these sites). Type I restriction endonucleases occur as a complex with the methylase and a polypeptide that binds to the recognition site on DNA. They are often not very specific and cut at a remote site. Type II restriction endonucleases are the classic experimental tools. They have very specific recognition and cutting sites. The recognition sites are short, 4-8 nucleotides and are usually palindromic sequences. Because both strands have the same sequence running in opposite directions the enzymes make double stranded breaks, which, if the site of cleavage is off centre, generates fragments with short single stranded tails, these can hybridise to the tails of other fragments and are called sticky ends. They are generally named according to the bacterium from which they were isolated (first letter of genus name and the first two letters of the specific name). The bacterial strain is identified next and multiple enzymes are given Roman numerals. For example the two enzymes isolated from the R strain of E. Coli are designated Eco RI and Eco RII. (10 Mar 1998) |
| restriction enzyme cutting site | <molecular biology> A specific nucleotide sequence of DNA at which a particular restriction enzyme cuts the DNA. Some sites occur frequently in DNA (for example, every several hundred basepairs), others much less frequently (rare-cutter, for example, every 10,000 base pairs). (10 Mar 1998) |
| restriction enzyme, endonuclease | A protein that recognises specific, short nucleotide sequences and cuts DNA at those sites. Bacteria contain over 400 such enzymes that recognise and cut over 100 different DNA sequences. See restriction enzyme cutting site. (05 Mar 2000) |
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