| ¿µ¹® | amino acids | ÇÑ±Û | ¾Æ¹Ì³ë»ê |
|---|---|---|---|
| ¼³¸í | ¾Æ¹Ì³ë±â(£NH3)¿Í Ä«¸£º¹½Ç±â(£COOH)¸¦ °¡Áö°í ÀÖ´Â ¸ðµç À¯±â¹°Áú. ´Ü¹éÁúÀ» ÀÌ·ç´Â ±âº»´ÜÀ§°¡ µÈ´Ù. Áï ´Ü¹éÁúÀº ¾Æ¹Ì³ë»êÀÌ ¿¬°áµÇ¾î¼ ÀÌ·ç´Â °ÍÀÌ´Ù. ÀÎü¿¡¼´Â ¾Æ¹Ì³ë»êÀÌ ´Ü¹éÁúÀÇ ±âº»´ÜÀ§°¡ µÇ´Â °Í¿Ü¿¡ ½Å°æ¼¼Æ÷¿Í ½Å°æ¼¼Æ÷°¡ ¼·Î ¿¬¶ôÀ» ÁÖ°í ¹Þ´Âµ¥ ¾²ÀÌ´Â ½Å°æÀü´Þ¹°Áú·Î¼ÀÇ ¿ªÇÒµµ ÇÑ´Ù. »ç¶÷ÀÇ ´Ü¹éÁúÀº 20°¡ÁöÀÇ ¾Æ¹Ì³ë»êÀ¸·Î ±¸¼ºµÈ´Ù. Áï »ç¶÷¿¡ ÀÖ¾î¼ ´Ü¹éÁúÀ» ÇÕ¼ºÇÏ´Â µ¥´Â 20°¡ÁöÀÇ ¾Æ¹Ì³ë»êÀÌ ÇÊ¿äÇÏ´Ù. ¿©±â¿¡¼ 11°¡Áö´Â ÀÎü³»¿¡¼ Á÷Á¢ ÇÕ¼ºÇÒ ¼ö ÀÖÁö¸¸ ³ª¸ÓÁö 9°¡Áö´Â ÇÕ¼ºÇÒ ¼ö ¾ø°í ¹Ýµå½Ã À½½Ä¹°¿¡¼ ¼·ÃëÇØ¾ß ÇÑ´Ù. À̰ÍÀ» Çʼö¾Æ¹Ì³ë»êÀ̶ó°í ÇÑ´Ù. |
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| ¿µ¹® | Dilatation and Curettage(D & C) | ÇÑ±Û | Àڱñܾ¼ú, ÀڱøñÈ®Àå |
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| ¼³¸í | ÀÚ±ÃÀ̶õ žư¡ ¼öÅÂµÇ¾î¼ ºÐ¸¸Àü±îÁö ¹ßÀ°ÇÏ°í ¼ºÀåÇÏ´Â °ø°£ÀÌ´Ù. Àڱüӿ¡ º´º¯ÀÌ ÀÖ¾î ÀÓ½ÅÀÌ °è¼ÓµÉ ¼ö ¾ø°Å³ª ¾Æ´Ï¸é ´Ù¸¥ ÀÌÀ¯·Î ÀӽŵǾî Àִ žƸ¦ Á¦°ÅÇϰíÀÚ ÇÒ °æ¿ì¿¡ »ç¿ëµÇ´Â ¹æ¹ýÀÌ´Ù. ¿©±â¼ ±Ü¾î³»±â À§ÇÏ¿©´Â ¿ì¼± ÀÚ±ÃÀÇ ÀÔ±¸¿¡ ÇØ´çÇÏ´Â ÀڱøñÀ» È®Àå½ÃÄÑ¾ß ÇÑ´Ù. ¿©±â¿¡´Â ±Þ¼ÓÈ÷ È®ÀåÀ» ½ÃµµÇÏ´Â ¹ý°ú ¼¼È÷ È®ÀåÀ» ½ÃµµÇÏ´Â 2°¡Áö ¹æ¹ýÀÌ ÀÖ´Ù. ÀڱøñÀ» ±Þ¼ÓÈ÷ È®ÀåÇÒ ¶§´Â Çì°¡¸£ ¸ñ°üÈ®Àå±â(Hegar's dilatator)¸¦ »ç¿ëÇÑ´Ù. À̰ÍÀº ÀÛÀº ±Ý¼Ó¸·´ë·Î ÀÛÀº Å©±âºÎÅÍ Å« Å©±â±îÁö ´Ù¾çÇÑ Å©±â°¡ ÀÖ¾î¼ ¿ì¼± ÀÛÀº ¸·´ë·Î ½ÃÀÛÇÏ¿© Á¡Á¡ Å« Å©±âÀÇ ¸·´ë¸¦ Àڱøñ¿¡ ³Ö¾î¼ ÀڱøñÀ» È®Àå½ÃŲ´Ù. ¼¼È÷ È®Àå½Ãų ¶§´Â Laminaria tent¸¦ ¸ñ°ü¿¡ »ðÀÔÇÏ´Â ¹æ¹ýÀ» »ç¿ëÇÑ´Ù. Laminaria tent¶õ ÇØÃÊ·Î ¸¸µç ÀÛÀº ¸·´ë·Î ¼öºÐÀ» Èí¼öÇϸé Á¡Á¡ ´Ã¾î³ª´Â ¼ºÁúÀÌ ÀÖ´Ù. À̰ÍÀ» ÀÚ±ÃÀÇ ¸ñ¿¡ ³ÖÀ¸¸é À̰ÍÀÌ ¼öºÐÀ» Èí¼öÇÏ¿© ´Ã¾î³ª¹Ç·Î õõÈ÷ ÀÚ±ÃÀÇ ¸ñÀÌ ´Ã¾î³´Ù. ÀڱøñÀÌ ÃæºÐÈ÷ ´Ã¾î³ª¸é ±× ¼ÓÀ¸·Î ³¡ÀÌ ¼ù°¡¶ôó·³ »ý±ä ±â±¸¸¦ ³Ö¾î¼ ÀڱüÓÀÇ º´º¯À̳ª ÀÓ½ÅµÈ Å¾Ƹ¦ ±Ü¾î³»´Âµ¥ ¿©±â¿¡ »ç¿ëµÇ´Â ¼ù°¡¶ôó·³ »ý±ä ±â±¸¸¦ Å¥·¿À̶ó°í ÇÑ´Ù. Ãʱâ ÀÓ½ÅÁßÀý Áï À¯»ê°ú °°Àº ÀӽŰú °ü·ÃµÈ °æ¿ì»Ó¸¸ ¾Æ´Ï¶ó, ºñÀӽŠÀÚ±ÃÀÇ Àڱ󻸷Á¶Á÷ÀÇ Ã¤Ãë ¹× Á¦°Å¸¦ À§Çؼµµ ÇàÇØÁö´Â ¼ö±âÀÌ´Ù. ÀÌ´Â ¿øÄ¢ÀûÀ¸·Î ¸¶ÃëÇÏ¿¡ ½Ç½ÃµÇ´Â °ÍÀ¸·Î Àڱøñ°üÀ» È®ÀåÇÏ°í ±â±¸·Î Àڱà ³»¿ë¹°À» Á¦°ÅÇϰí Å¥·¿À¸·Î Àڱ󻺮À» ±ú²ýÀÌ ÇÑ´Ù. ÀÚ±Ãõ°øÀ̳ª ÀڱøñÀÇ ÆÄ¿ µîÀÇ À§ÇèÀÌ µû¸£¸ç, ¼ö¼úÈÄ °¨¿° ¶Ç´Â ÃâÇ÷ µî¿¡ ´ëÇÑ ÁÖÀǰ¡ ÇÊ¿äÇÏ´Ù. |
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| ¿µ¹® | serum proteins | ÇÑ±Û | Ç÷û´Ü¹é |
|---|---|---|---|
| ¼³¸í | Ç÷û¿¡ ÀÖ´Â ´Ü¹éÁúµéÀ» ÃÑĪÇÏ´Â ¸»·Î, ¸é¿ª±Û·ÎºÒ¸°(¸é¿ªÇö»ó¿¡ °ü¿©ÇÏ´Â Ç×ü¸¦ Çü¼ºÇÔ), ¾ËºÎ¹Î, º¸Ã¼ ¹× ÀÀ°íÀÎÀÚ¿Í ¿©·¯ È¿¼ÒµéÀÌ ÀÌ¿¡ ¼ÓÇÑ´Ù. |
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| TAGH | triiodothyronine, amino acids, glucagon, and heparin |
|---|---|
| GnRH | Gonadotropin Releasing Hormone [HP 1898, 2034] = LHRH = Go... |
| CAA | carotid audiofrequency analysis; cerebral amyloid angiopathy; circulating anodic antigen; Clean Air ... |
| PVM | pneumonia virus of mice; proteins, vitamins, and minerals |
| PBPs | Penicillin-Binding Proteins |
| G proteins | GIP-binding proteins |
|---|---|
| G-proteins | GTP)-binding regulatory proteins |
| G-proteins | Guanine nucleotide-binding regulatory proteins |
| G proteins | reglatory proteins |
| BLP | Bombesin-like peptides |
para-amino salicylic acid
acute angle
| amino acids, peptides, and proteins | Amino acids and chains of amino acids connected by peptide linkages. (12 Dec 1998) |
|---|
| amino acids | Organic compounds that generally contain an amino (-nh2) and a carboxyl (-cooh) group. Twenty alpha-amino acids are the subunits which are polymerised to form proteins. (12 Dec 1998) |
|---|---|
| amino acids, branched-chain | Amino acids which have a branched carbon chain. (12 Dec 1998) |
| amino acids, cyclic | A class of amino acids characterised by a closed ring structure. (12 Dec 1998) |
| essential amino acids | Alpha-amino acids nutritionally required by an organism and which must be supplied in its diet (i.e., cannot be synthesised by the organism) either as free amino acid or in proteins. (05 Mar 2000) |
| excitatory amino acids | Endogenous amino acids released by neurons as excitatory neurotransmitters. Glutamic acid is the most common excitatory neurotransmitter in the brain. Aspartic acid has been regarded as an excitatory transmitter for many years, but the extent of its role as a transmitter is unclear. (12 Dec 1998) |
| bitter peptides | Peptides that have a bitter taste and may spoil certain foods; often contain high proportions of leucyl, valyl, and aromatic amino acid residues. (05 Mar 2000) |
| peptides | Any member of a class of compounds of low molecular weight which yield two or more amino acids on hydrolysis. Formed by loss of water from the nh2 and cooh groups of adjacent amino acids, they are known as di-, tri-, tetra- (etc.) peptides, depending on the number of amino acids in the molecule. Peptides form the constituent parts of proteins. (12 Dec 1998) |
| signal peptides | Additional polypeptide sequence of 25 to 30 residues at the amino-terminal or carboxy-terminal end of proteins. The signal sequence signals the cellular fate or destination of a newly synthesised protein directing it to its ultimate destination in the cell. These leaders are recognised by the signal recognition particle and bound by specific receptor sites on the outer surface of the endoplasmic reticulum. They are then transported into the cisterna of the endoplasmic reticulum and from there directed to their ultimate destination in the cell. In prokaryotes, the signal peptides attach to the plasma membrane. These signal sequences are ultimately removed by specific peptidases. (12 Dec 1998) |
| opioid peptides | The endogenous peptides with opiate-like activity. The three major classes currently recognised are the enkephalins, the dynorphins, and the endorphins. Each of these families derives from different precursors, proenkephalin, prodynorphin, and pro-opiomelanocortin, respectively. There are also at least three classes of opioid receptors, but the peptide families do not map to the receptors in a simple way. (12 Dec 1998) |
| bile acids and salts | <chemical> Steroid acids and salts. The primary bile acids are derived from cholesterol in the liver and usually conjugated with glycine or taurine. The secondary bile acids are further modified by bacteria in the intestine. They play an important role in the digestion and absorption of fat. They have also been used pharmacologically, especially in the treatment of gallstones. Pharmacological action: cholagogues and choleretics, gastrointestinal agents. (12 Dec 1998) |
| nucleic acids, nucleotides, and nucleosides | Complex compounds of high molecular weight occurring in living cells. These are basically of two types, ribonucleic (RNA) and deoxyribonucleic (DNA) acids, both of which consist of nucleotides (nucleoside phosphates linked together by phosphate bridges). (12 Dec 1998) |
| acidic amino acid | An Amino acid with a second acid moiety, e.g., glutamic acid, aspartic acid, cysteic acid. (05 Mar 2000) |
| activated amino acid | The product formed by the condensation of the acyl radical of an amino acid and adenosine 5'-monophosphate (originally in the form of adenosine 5'-triphosphate, with elimination of a pyrophosphoric group). Formed in the first step of protein biosynthesis. Synonym: activated amino acid. (05 Mar 2000) |
| alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid | <chemical> Alpha-amino-2,3-dihydro-5-methyl-3-oxo-4-isoxazolepropanoic acid. An ibotenic acid homolog and glutamate agonist. The compound is the defining agonist for the ampa subtype of glutamate receptors (receptors, ampa). It has been used as a radionuclide imaging agent but is more commonly used as an experimental tool in cell biological studies. Pharmacological action: excitatory amino acid agonists. Chemical name: 4-Isoxazolepropanoic acid, alpha-amino-2,3-dihydro-5-methyl-3-oxo- (12 Dec 1998) |
| alpha-amino acid | Typically, an amino acid of the general formula R-CHNH2-COOH (i.e., the NH2 in the a position); the l forms of these are the hydrolysis products of proteins. In rarer usages, this class of molecules also includes alpha-amino phosphoric acids and alpha-aminosulfonic acids. (05 Mar 2000) |
Synonyms :
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