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"amino acid accepting RNA"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
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  • ¿µ¹®
    ÇѱÛ
  • heteropoly acid
    ÇìÅ׷δÙÁß»ê
  • hippuric acid
    È÷Ǫ¸£»ê, ¸¶´¢»ê
  • homogentisic acid
    È£¸ð°ÕƼ½Å»ê
  • humic acid
    È޹λê
  • hyaluronic acid
    È÷¾Ë·ç·Ð»ê
  • hydrochloric acid
    ¿°»ê
  • hydrocyanic acid
    È÷µå·Î½Ã¾È»ê
  • hydrofluoric acid
    ºÒÈ­¼ö¼Ò»ê
  • hydroxyindoleacetic acid
    È÷µå·Ï½ÃÀε¹¾Æ¼¼Æ®»ê
  • isothiocyanic acid
    ÀÌ¼ÒÆ¼¿À½Ã¾È»ê
  • inosinic acid
    À̳ë½Å»ê
  • ketonic acid
    ÄÉÅæ»ê
  • lauric acid
    ·Î¸£»ê
  • leuconic acid
    ·ùÄÜ»ê
  • lichenic acid
    ÁöÀÇ»ê
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  • ¿µ¹®
    ÇѱÛ
  • linolenic acid
    ¸®³î·»»ê
  • linolic acid
    ¸®³î»ê
  • lipoic acid
    ¸®Æ÷»ê
  • maleic acid
    ¸»·¹»ê
  • malic acid
    ¸»»ê
  • malonic acid
    ¸»·Ð»ê
  • mixed acid
    È¥ÇÕ»ê
  • mucic acid
    ¹Â½Å»ê
  • muramic acid
    ¹Â¶ó¹Í»ê
  • mycolic acid
    ¹ÌÄÝ»ê
  • neuraminic acid
    ´º¶ó¹Î»ê
  • neurostearic acid
    ½Å°æÁö¹æ»ê
  • nicotinic acid
    ´ÏÄÚÆ¾»ê
  • nitric acid
    Áú»ê
  • nitrobenzoic acid
    ³ªÀÌÆ®·Îº¥Á¨»ê
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  • ¿µ¹®
    ÇѱÛ
  • acid perfusion
    »ê°ü·ù(߫δêü), »êȯ·ù.
  • acid phosphatase
    »ê¼ºÆ÷½ºÆÄŸÁ¦
  • acid phosphatase
    »ê¼ºÆ÷½ºÆÄÅ×À̽ºÁ¦.
  • acid phosphatase
    »ê¼º Æ÷½ºÆÄÅ×À̽º(ß«àõ¡­)
  • acid phosphatase
    »ê¼ºÀλêÈ¿¼î
  • acid phosphatase assay
    »ê¼ºÆ÷½ºÆÄŸÁ¦ ÃøÁ¤
  • acid pyuria
    »ê¼º ³ó´¢
  • acid radical
    »ê±â(ß«Ðñ).
  • acid salt
    »ê¼º¿°(ß«àõç¤).
  • acid springs
    »ê¼ºÃµ(Ë×ËÛ̧).
  • acid sterile pyuria
    »ê¼º¹«±Õ³ó´¢
  • acid tide
    »êÁõ°¡±â.
  • acid value
    »ê°ª, »ê°¡(߫ʤ).
  • acid, dipicolinic
    µðÇÇÄݸ°»ê
  • acid, lipoteichoic
    ÁöÁúŸÀÌÄÚ»ê
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  • ¿µ¹®
    ÇѱÛ
  • acid-base buffer system
    »ê¿°±â¿ÏÃæ°è
  • acid-base compensation
    »ê¿°±â º¸»ó
  • acid-base indicator
    »ê¿°±âÁö½Ã¾à
  • acid-fast bacillus
    Ç×»ê±Õ(ù÷߫ж)
  • acid-fast stain
    Ç׻꼺 ¿°»ö
  • acid-fast stain
    Ç׻꼺¿°»ö(ù÷ß«àõæøßä)
  • acid<³ª> acidus
    »ê(ß«), »ê¼º(ß«àõ)ÀÇ.
  • adenylic acid deaminase
    ¾Æµ¥´Ò»ê Å»¾Æ¹Ì³ëÈ¿¼Ò.
  • aliphatic acid
    Áö¹æÁ·»ê(ò·Û¸ðéß«).
  • allokainic acid
    ¾Ë·ÎÄ«Àλê(¡­ß«).
  • aloetic acid
    ¾Ë·Î¿¡Æ¾»ê.
  • alpha1-acid glycoprotein
    ¾ËÆÄ-»ê´ç´Ü¹é
  • aminoacetic acid<³ª> acidum aminoaceticum
    ¾Æ¹Ì³ë¾Æ¼¼Æ®»ê.
  • aminohippuric acid
    ¾Æ¹Ì³ë ¸¶´¢»ê
  • anaphylaxis,arachidonic acid metabolitesin
    ¾Æ¶ó۵·»ê ´ë»ç¹°Áú(¡­ß« ÓÛÞóÚªòõ)
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  • ¿µ¹®
    ÇѱÛ
  • recombinant RNA technique
    ÀçÁ¶ÇÕ(î¢ðÚùê) RNA ¼ú(âú)
  • ribosomal precursor RNA
    ¶óÀ̺¸¼Ø Àü±¸(îñÏÌ) RNA
  • ribosomal RNA
    ¶óÀ̺¸¼Ø RNA
  • RNA
    (å²) Ribonucleic acid
  • RNA-11
    ( å²) Ribonucleic acid-11 (ÔÒ) A-RNA
  • RNA coding triplet
    RNA ºÎÈ£(ݬûÜ)»ïÁßÇ×(ß²ñìú£)
  • RNA-dependent (directed) DNA polymerase
    RNA ÀÇÁ¸(ëîðí)(Áö½Ã(ò¦ãÆ)) DNA Æú¸®¸Ó·¹À̽º
  • RNA dot blot
    RNA Á¡(ïÇ)ºí·Ô
  • RNA-driven hybridization
    RNA ÁÖµ¿(ñ«ÔÑ) ÇÏÀ̺긮µåÈ­(ûù)
  • RNA gene
    RNA À¯ÀüÀÚ(ë¶îîí­)
  • RNA ligase
    RNA ¶óÀ̰ÔÀ̽º
  • RNA maturation
    RNA ¼º¼÷(à÷âÙ)
  • RNA modification
    RNA ¼ö½Ä(áóãÞ)
  • RNA nucleotidyltransferase
    RNA ´©Å¬·¹¿ÀŸÀ̵ô Æ®¶õ½ºÆÛ·¹À̽º
  • RNA phage
    RNA ÆÄÁö
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 8
BCT brachiocephalic trunk; branched-chain amino acid transferase
CAAX [box] protein segment in which C is cysteine, A is usually but not always an aliphatic amino acid, and X i...
EAAC excitatory amino acid carrier
GABOA gamma-amino-beta-hydroxybutyric acid
GOBAB gamma-hydroxy-beta-amino-butyric acid
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 8
D(-)AP5 D(-)-2-amino-5-phosphonopentanoic acid
D(-)APV D(-)-2-amino-5-phosphonovaleric acid
D(-)AP5 D(-)2-amino-5-phosphonovaleric acid
D-AAO D-Amino acid oxidase
DAO D-Amino acid oxidase
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • kinotannic acid
    Ű³ëź´Ñ»ê
  • laccainic acid
    ¶óÄ«ÀÎ »ê
    Àû°¥»öÀÇ °áÁ¤ »ê.
  • laccic acid
    ¶óÅ© »ê
    ¶óÅ© ¿°·á¿¡¼­ ¾ò´Â Àû°¥»öÀÇ °áÁ¤¹°.
  • lactic acid
    À¯»ê
    Ä«¸£º¹½Ã±â, ¼ö»ê±â, ¸ÞÆ¿±â, ¼ö¼ÒÀÇ ³× ¿øÀÚ´ÜÀÌ °áÇÕÇÑ ºñ´ëĪ ź¼Ò ¿øÀÚ¸¦ °¡Áö´Â À¯±âÈ­ÇÕ¹°. È÷µå·Ï½Ã ÇÁ·ÎÇǿ»ê, ¶ôÆ®»ê, À¯»êÀ̶ó°íµµ ÇÑ´Ù. 1780³â K.W. ¼Ð·¹¿¡ ÀÇÇØ »êÆÐÇÑ ¿ìÀ¯ ¼Ó¿¡¼­ ¹ß°ßµÇ¾úÀ¸¸ç µ¿½Ä¹°°è¿¡ ³Î¸® Á¸ÀçÇÑ´Ù. D, L, DLÇüÀÇ ±¤ÇÐ À̼ºÁúü°¡ ÀÖ´Ù. L-Á¥»êÀº ÇØ´ç °úÁ¤ÀÇ ÃÖÁ¾ »ê¹°·Î¼­ ÇÇ·çºê»êÀÇ È¯¿ø¿¡ ÀÇÇØ »ý¼ºµÈ´Ù. Á¶ÇؼºÀÌ °­ÇÑ ÁÖ»ó °áÁ¤À̸ç, ³ì´ÂÁ¡Àº 25¡­26 ¡ÉÀÌ´Ù. ±ÙÀ°, µ¿¹°Á¶Á÷ ¼Ó¿¡ Á¸ÀçÇÏ¸ç »ç¶÷ÀÇ Ç÷¾× ¼Ó¿¡´Â 100 m§¤´ç 5¡­20 mgÀÌ Á¸ÀçÇϸç, ½ÉÇÑ ¿îµ¿¿¡ ÀÇÇØ Áõ°¡ÇÑ´Ù. ¿îµ¿¿¡ ÀÇÇÑ ±ÙÀ°ÀÇ ÇǷδ ±Û¸®ÄÚ°ÕÀÇ ºÐÇØ¿¡ ÀÇÇÑ L-Á¥»êÀÇ ÃàÀû°ú °ü°è°¡ ÀÖ´Ù. ÈÞ½Ä ½Ã¿¡´Â ±× ÀϺΰ¡ »êÈ­ ºÐÇØµÇÁö¸¸ ´ëºÎºÐ ¿ø·¡ÀÇ ±Û¸®ÄÚ°ÕÀ¸·Î ÀçÇÕ¼ºµÈ´Ù. D-Á¥»êÀº µÎ²¨¿î ÆÇ»ó °áÁ¤À̸ç, ³ì´ÂÁ¡Àº 26¡­27 ¡ÉÀÌ´Ù. DL-Á¥»ê
  • lactic acid bacteria
    Á¥»ê ±Õ
    ±Û·çÄÚ¿À½º µî ´ç·ù¸¦ ºÐÇØÇÏ¿© Á¥»êÀ» »ý¼ºÇÏ´Â ¼¼±Õ. ¶ôÆ®»ê±Õ, À¯»ê ±ÕÀ̶ó°íµµ ÇÑ´Ù. Á¥»ê ¹ßÈ¿¿¡ ÀÇÇØ »ý¼ºµÇ´Â Á¥»ê¿¡ ÀÇÇØ¼­ º´¿ø ±Õ°ú À¯ÇØ ¼¼±ÕÀÇ »ýÀ°ÀÌ ÀúÁöµÇ´Â ¼ºÁúÀ» À¯Á¦Ç°
  • lactic acid bacterium
    ¶ôÆ® ±Õ
  • lactic acid formation
    À¯»ê Çü¼º
  • lactonic acid
    ¶ôÅæ »ê
    À¯´ç. ¾Æ¶óºñ¾Æ °í¹«. °¥¶ôÅ佺¸¦ »êÈ­ÇÔÀ¸·Î½á ¾ò¾îÁø´Ù.
  • lanopalmic acid : ¾ç¸ðÁö¿¡ µé¾î ÀÖ´Â 1¼ö»ê±â¼ºÀÇ Æ÷È­ Áö¹æ»ê.

    lanosterol

    ¶ó³ë½ºÅ×·Ñ
    ¾ç¸ðÁö¿¡ µé¾î ÀÖ´Â ½ºÅ×·ÑÀÇ ÀÏÁ¾.
  • larinolic acid
    ¶ó¸®³î »ê
  • linolic acid
    ¸®³î»ê
  • lymphocantric acid
    ¸²Æ÷Ä­Æ®¸£»ê
    Àӯļº ¹éÇ÷º´ ȯÀÚÀÇ ¿ä¿¡¼­ ÃßÃâµÈ´Ù.
  • lysalbinic acid
    ¸®»ìºó »ê
    ³­¹éÀ» °¡¼º ¼Ò¿À´Ù·Î ó¸®ÇÔÀ¸·Î½á ¾ò¾îÁö´Â »ê.
  • lysergic acid
    ¸®À縣±×»ê
    ¸Æ°¢ ¾ËÄ®·ÎÀ̵åÀÇ ¸ðü·Î, ±× À̼ºÃ¼ÀÎ ÀÌ¼Ò ¸®Á¦¸£±×»ê°ú ÇÔ²² Æ®¸®ÆéƼµå ¶Ç´Â ¾Æ¹Ì³ë ÇÁ·ÎÆÄ³î°ú °áÇÕÇÏ¿© ¸Æ°¢ ¾ËÄ®·ÎÀ̵å·ù¸¦ Çü¼ºÇÑ´Ù.
  • lyxonic acid
    ¸¯¼Õ»ê
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 8
RNA ligase <enzyme> An enzyme that catalyses the conversion of linear RNA to a circular form by the transfer of the 5'-phosphate to the 3'-hydroxyl terminus. It also catalyses the covalent joining of two polyribonucleotides in phosphodiester linkage.
Chemical name: Poly(ribonucleotide):poly(ribonucleotide)ligase (AMP-forming)
Registry number: EC 6.5.1.3
(12 Dec 1998)
RNA N-glycosidase <enzyme> Catalyses hydrolysis of a single adenosine glycosidic bond; probable cause of toxic effect of vero toxin from E coli by inactivating 60s ribosomal subunit
Registry number: EC 3.2.2.-
Synonym: RNA glycosylase
(26 Jun 1999)
RNA, nuclear RNA molecules found in the nucleus either associated with chromosomes or in the nucleoplasm.
(12 Dec 1998)
RNA nucleotidyltransferases <enzyme> Enzymes that catalyze the template-directed incorporation of ribonucleotides into an RNA chain.
Registry number: EC 2.7.7.
(12 Dec 1998)
RNA phages Bacteriophages whose genetic material is RNA, which is single-stranded in all except the pseudomonas phage phi6. All RNA phages infect their host bacteria via the host's surface pili. Some frequently encountered RNA phages are: qbeta, ms2, bf23, f2, r17, fr, mu2, phicb5, phicb12r, phicb8r, phicb23r, 7s, phi6, pp7.
(12 Dec 1998)
RNA, plant Ribonucleic acid in plants having regulatory and catalytic roles as well as involvement in protein synthesis.
(12 Dec 1998)
RNA plasmid <molecular biology> DsRNA found in yeasts, also called killer factors. Their nomenclature is uncertain and some scientists consider them viruses.
(23 Aug 1998)
RNA polymerase <enzyme, molecular biology> An enzyme that polymerise ribonucleotides in accordance with the information present in DNA.
Prokaryotes have a single enzyme for the three RNA types that is subject to stringent regulatory mechanisms. Eukaryotes have type I that synthesises all rRNA except the 5S component, type II that synthesises mRNA and hnRNA and type III that synthesises tRNA and the 5S component of rRNA.
(23 Aug 1998)
RNA polymerase I <enzyme> A DNA-dependent RNA polymerase present in bacterial, plant, and animal cells. The enzyme functions in the nucleolar structure and transcribes DNA into RNA. It has different requirements for cations and salts than RNA polymerase II and III and is not inhibited by alpha-amanitin.
Registry number: EC 2.7.7.-
(12 Dec 1998)
RNA polymerase II <enzyme> A DNA-dependent RNA polymerase present in bacterial, plant, and animal cells. It functions in the nucleoplasmic structure and transcribes DNA into RNA. It has different requirements for cations and salt than RNA polymerase I and is strongly inhibited by alpha-amanitin.
Registry number: EC 2.7.7.-
(12 Dec 1998)
RNA polymerase III <enzyme> A DNA-dependent RNA polymerase present in bacterial, plant, and animal cells. It functions in the nucleoplasmic structure where it transcribes DNA into RNA. It has specific requirements for cations and salt and has shown an intermediate sensitivity to alpha-amanitin in comparison to RNA polymerase I and II.
Registry number: EC 2.7.7.-
(12 Dec 1998)
RNA precursors RNA copies from DNA that exactly represent the genome sequence. This RNA cannot be used for producing protein until RNA splicing takes place. During this procedure the phosphodiester bonds at exon-intron boundaries are cleaved and the intron is excised. Consequently a new bond is formed between the ends of the exons. The resulting RNA is mature RNA which can be translated into protein.
(12 Dec 1998)
RNA primase <enzyme, molecular biology> An RNA polymerase that synthesises a short RNA primer sequence to initiate DNA replication.
(18 Nov 1997)
RNA primer <molecular biology> The primer sequence synthesised by RNA primase.
(23 Aug 1998)
RNA probes RNA, usually prepared by transcription from cloned DNA, which complements a specific mRNA or DNA and is generally used for studies of virus genes, distribution of specific RNA in tissues and cells, integration of viral DNA into genomes, transcription, etc. Whereas DNA probes are preferred for use at a more macroscopic level for detection of the presence of DNA/RNA from specific species or subspecies, RNA probes are preferred for genetic studies. Conventional labels for the RNA probe include radioisotope labels 32p and 125i and the chemical label biotin. RNA probes may be further divided by category into plus-sense RNA probes, minus-sense RNA probes, and antisense RNA probes.
(12 Dec 1998)
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