| ¿µ¹® | deoxyribonucleic acid (DNA) | ÇÑ±Û | µ¥¿Á½Ã¸®º¸ÇÙ»ê |
|---|---|---|---|
| ¼³¸í | ÇÙ»êÀÇ ÀÏÁ¾À¸·Î DNA¶ó°íµµ ÇÑ´Ù. DeoxyribonucleotideÀÇ ÁßÇÕüÀ̸ç À¯ÀüÀÚÀÇ ÈÇÐÀû º»Ã¼ÀÌ´Ù. RNA¹ÙÀÌ·¯½º ÀÌ¿ÜÀÇ ¸ðµç »ý¹°Àº DNA¸¦ À¯ÀüÀÚ·Î Áö´Ï°í ÀÖ´Ù. µð¿Á½Ã¸®º¸´ºÅ¬·¹¿ÀƼµå(deoxyribonucleotide)´Â ¿°±â¿Í ´ç(2'-deoxy-D-ribose)°ú ÀλêÀ¸·Î ÀÌ·ç¾îÁø´Ù. ¿°±â´Â ¾Æµ¥´Ñ(adenine), ±¸¾Æ´Ñ(guanine), Ƽ¹Î(thymine)¹× ½ÃÅä½Å(cytosine)ÀÇ 4°¡ÁöÀ̸ç, À̰ÍÀº ´ç¿¡ ºÎÂøµÇ¾î ÀÖ´Ù. ÀÎ»ê ¿ª½Ã ´çÀÇ ÇÑ ºÎºÐ¿¡ ºÎÂøµÇ¾î ÀÖ´Ù. ÀÌ deoxyribonucleotideÀÇ ´çÀº ´Ù¸¥ deoxy- ribonucleotideÀÇ ´ç°ú ÀλêÀ» »çÀÌ¿¡ ³õ°í °áÇÕÀ» ÇÏ°Ô µÇ¾î ÇϳªÀÇ ±ä »ç½½À» Çü¼ºÇÏ°Ô µÈ´Ù. Áï ´ç°ú ÀλêÀÌ ÁÖÃàÀÌ µÇ¾î¼ deoxyribonucleotideÀÇ ±ä »ç½½À» ¸¸µç´Ù. ÀÌ deoxyribonucleotideÀÇ »ç½½ µÎ °³´Â °¢°¢ deoxyribonucleotide¿¡ ºÎÂøµÇ¾î ÀÖ´Â ¿°±âµéÀÌ °áÇÕÀ» ÇÏ¿© µÎ °³ÀÇ »ç½½ÀÌ °áÇյǾî ÀÖ´Â ÀÌÁß³ª¼± ±¸Á¶¸¦ ¸¸µé°Ô µÈ´Ù. 4°¡Áö ¿°±â ¾Æµ¥´ÑÀº Ƽ¹Î°ú °áÇÕÀ» Çϰí, ½ÃÅä½Å°ú °áÇÕÀ» ÇÏ°Ô µÈ´Ù. Áï ´ç°ú ÀλêÀº ±ä »ç½½À» ¸¸µå´Â ¿ªÇÒÀ» ÇÏ°í ±ä »ç½½¿¡ ºÎÂøµÈ ¿°±âµéÀÇ °áÇÕ¿¡ ÀÇÇØ¼ µÎ °³ÀÇ ±ä »ç½½Àº ¼·Î ºÙ¾î¼ ÀÌÁß³ª¼± ±¸Á¶¸¦ ¸¸µç´Ù. DNAÀÇ À¯ÀüÁ¤º¸´Â ¿°±â¿¡ ÀúÀåµÈ´Ù. 4°³ÀÇ ¿°±âÀÇ Á¶ÇÕ°ú ¹è¿ÀÌ À¯ÀüÁ¤º¸¸¦ º¸°üÇÏ´Â ÇϳªÀÇ ¾ÏÈ£ ¿ªÇÒÀ» ÇàÇÏ°Ô µÈ´Ù. |
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| ¿µ¹® | DNA | ÇÑ±Û | µð¿Á½Ã¸®º¸ÇÙ»ê, µð¿£¿¡ÀÌ |
|---|---|---|---|
| ¼³¸í | Deoxyribonucleic acidÀÇ ¾à¾î. µ¥¿Á½Ã¸®º¸½º¸¦ ±¸¼º¼ººÐÀ¸·Î ÇÏ´Â ÇÙ»ê. À¯ÀüÀÚÀÇ ÈÇÐÀû º»Å·μ ¿°»öü¿¡ Á¸ÀçÇÑ´Ù. µ¥¿Á½Ã¸®º¸½º¿¡ À¯±â¿°±â¿Í ÀλêÀÌ °áÇÕÇÑ ´ºÅ¬·¹¿ÀƼµå(±¸¼º´ÜÀ§)°¡ Æ÷½ºÆ÷µð¿¡½ºÅ׸£°áÇÕ¿¡ ÀÇÇØ ±ä»ç½½ ÁßÇÕü¸¦ Çü¼ºÇϸç, µÎ °³ÀÇ ±ä»ç½½ÀÌ ¼·Î ºñƲ·Á ²¿ÀÎ ³ª¼±±¸Á¶¸¦ ÃëÇÑ´Ù. µð¿Á½Ã¸®º¸´ºÅ¬·¹¿ÀƼµå(deoxyribonucleotide)´Â ¿°±â¿Í ´ç(2'-deoxy-D-riboe)°ú ÀλêÀ¸·Î ÀÌ·ç¾îÁø´Ù. ¿°±â´Â ¾Æµ¥´Ñ(adenine), ±¸¾Æ´Ñ(guanine), Ƽ¹Î(thymine) ¹× ½ÃÅä½Å(cytosine)ÀÇ ³×°¡ÁöÀ̸ç, À̰ÍÀº ´ç¿¡ ºÎÂøµÇ¾î ÀÖ´Ù. ÀÎ»ê ¿ª½Ã ´çÀÇ ÇÑ ºÎºÐ¿¡ ºÎÂøµÇ¾î ÀÖ´Ù. ÀÌ µð¿Á½Ã¸®º¸´ºÅ¬·¹¿ÀƼµåÀÇ ´çÀº ´Ù¸¥ µð¿Á½Ã¸®º¸´ºÅ¬·¹¿ÀƼµåÀÇ ´ç°ú ÀλêÀ» »çÀÌ¿¡ ³õ°í °áÇÕÇÏ°Ô µÇ¾î ÇϳªÀÇ ±ä »ç½½À» Çü¼ºÇÏ°Ô µÈ´Ù. |
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| HELLP | hemolysis, elevated liver enzymes, and low platelet count [syndrome] |
|---|---|
| DNA | Deoxyribo-Nucleic Acid |
| DDS | damaged disc syndrome; dendrodendritic synaptosome; dental distress syndrome; depressed DNA synthesi... |
| DNA | deoxyribonucleic acid; did not answer |
| G1 | presynthetic gap [phase of cells prior to DNA synthesis] |
| CYPs | Cytochrome P450 enzymes |
|---|---|
| HELLP | Haemolysis, Elevated Liver Enzymes and Low Platelets |
| HELLP | Hemolysis, Elevated Liver enzymes, and Low Platelet count |
| SBE | Starch branching enzymes |
| UBCs | Ubiquitin conjugating enzymes |
IGF-II : insulin like growth factor-IIÀÇ ¾àÀÚ. ¸¹Àº Àå±â¿Í Á¶Á÷¿¡ ÀÛ¿ëÇÏ¿© ´Ü¹é ÇÕ¼º°ú DNA, RNAÀÇ ÇÕ¼ºÀ» Áõ°¡½ÃÄÑ ¼¼Æ÷ÀÇ ¼ö¿Í ¾çÀ» Áõ°¡
| 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) |
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| DNA restriction enzymes | <enzyme> Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded fragments with terminal 5'-phosphates. The function of restriction enzymes is to destroy any foreign DNA that invades the host cell. most have been studied in bacterial systems, but a few have been found in eukaryotic organisms. They are also used as tools for the systematic dissection and mapping of chromosomes, in the determination of base sequences of dnas, and have made it possible to splice and recombine genes from one organism into the genome of another. Registry number: EC 3.1.21 (12 Dec 1998) |
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| complement activating enzymes | <enzyme> Enzymes present in the complement system which activate one or more components in the system. Registry number: EC 3.- (12 Dec 1998) |
| hydrolyzing enzymes | <enzyme> Registry number: EC 3. (12 Dec 1998) |
| splitting enzymes | Enzyme's that, like aldolases, catalyze the conversion of a molecule into two smaller molecules without the addition or subtraction of any atoms. (05 Mar 2000) |
| deamidizing enzymes | <enzyme> Registry number: EC 3.5. (12 Dec 1998) |
| deaminating enzymes | Enzymes catalyzing simple hydrolysis of C-NH2 bonds of purines, pyrimidines, and pterins, usually named in terms of the substrate, e.g., guanine deaminases, adenosine deaminases, AMP deaminases, pterin deaminases and thus producing ammonia; not generally used for deamination of noncyclic amides. Deaminases are distinguished from ammonia-lyases (EC group 4.3.1) in that the latter produce an unsaturation at the point of NH3 removal. Synonym: deaminating enzymes. (05 Mar 2000) |
| debranching enzymes | Enzyme's that bring about destruction of branches in glycogen; formerly considered to be one enzyme, now known to be a mixture of transferases (4-alpha-d-glucanotransferase) and hydrolases (amylo-1,6-glucosidase). Synonym: debranching factors. (05 Mar 2000) |
| digestive enzymes | Enzymes that are utilised in the digestive system, enzymes that are hydrolases of macromolecules (e.g., amylases, proteinases). (05 Mar 2000) |
| transferring enzymes | <enzyme> Transferases are enzymes transferring a group, for example, the methyl group or a glycosyl group, from one compound (generally regarded as donor) to another compound (generally regarded as acceptor). The classification is based on the scheme "donor:acceptor group transferase". Registry number: EC 2. (12 Dec 1998) |
| enzymes, coenzymes, and enzyme inhibitors | Proteins or RNA that act as biological catalysts, their cofactors, and inhibitors. (12 Dec 1998) |
| enzymes, immobilised | Enzymes which are immobilised on or in a variety of water-soluble or water-insoluble matrices with little or no loss of their catalytic activity. Since they can be reused continuously, immobilised enzymes have found wide application in the industrial, medical and research fields. (12 Dec 1998) |
| DNA-directed DNA polymerase | <enzyme> DNA-dependent DNA polymerases found in bacteria, animal and plant cells. During the replication process, these enzymes catalyze the addition of deoxyribonucleotide residues to the end of a DNA strand in the presence of DNA as template-primer. They also possess exonuclease activity and therefore function in DNA repair. Chemical name: Deoxynucleoside-triphosphate:DNA deoxynucleotidyltransferase (DNA-directed) Registry number: EC 2.7.7.7 (12 Dec 1998) |
| A-DNA | A form of DNA in which the helix is right-handed and the overall appearance is short and broad. (05 Mar 2000) |
| a-form DNA | <molecular biology> One of several forms that can be assumed by a double helix. A-DNA is stable in dehydrated conditions. This form is less common than the dominant form found under physiological conditions -- beta-DNA. This form is also assumed by DNA-RNA hybrid helices and by regions of double-stranded RNA. It is a right-handed helix and is a more compact form than beta-DNA. (09 Oct 1997) |
| antisense DNA | <molecular biology> A synthetic DNA strand that is complementary to a particular strand of target DNA with a complementary sequence of bases. This results in preventing expression of the gene encoded. These proteins can be used to selectively turn off production of certain proteins or block viral genetic instructions, by marking them for destruction by cellular enzymes, in order to prevent the building of new virus or the infection of new cells. (14 Nov 1997) |
Synonyms : DNA Restriction Modification Enzymes, Restriction Modification Systems, Enzymes, DNA Restriction-Modification, Modification Systems, Restriction, Restriction-Modification Enzymes, DNA, Systems, Restriction Modification, Systems, Restriction-Modification
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