| ¿µ¹® | peptide | ÇÑ±Û | ÆéƼµå |
|---|---|---|---|
| ¼³¸í | µÎ °³ÀÌ»óÀÇ ¾Æ¹Ì³ë»ê ºÐÀÚ »çÀÌ¿¡¼, ÇÑÂÊÀÇ ¾Æ¹Ì³ë±â¿Í ´Ù¸¥ ÂÊÀÇ Ä«¸£º¹½Ç±â°¡ ¹° ºÐÀÚ¸¦ ÀÒÀ¸¸é¼ ÃàÇÕÇÏ¿© ÀÌ·ç´Â ¾Æ¹Ìµå °áÇվƹ̳ë»êÀÇ ¼ö°¡ 2, 3, ¡¦ ÀÎ °æ¿ì, °¢°¢ µðÆéƼµå, Æ®¸®ÆéƼµå, ¡¦µîÀ¸·Î ºÎ¸£¸ç, ¿©·¯ °³ÀÇ ¾Æ¹Ì³ë»êÀ¸·Î ±¸¼ºµÇ´Â °ÍÀ» ¿Ã¸®°íÆéƼµå, À̺¸´Ù Å« °ÍÀ» Æú¸®ÆéƼµå¶ó°í ÇÑ´Ù. Á÷¼â»óÀÇ °ÍÀÌ ¸¹Áö¸¸, ȯ»ó ±¸Á¶¸¦ °®´Â ÆéƼµåµµ ÀÖ´Ù. ÀúºÐÀÚÀÇ ÆéƼµå´Â ¹°, »ê, ¾ËÄ®¸® µûÀ§¿¡ Àß ³ì°í ¾ËÄڿÿ¡´Â ³ìÁö ¾ÊÀ¸³ª, °íºÐÀÚÀÇ ÆéƼµå´Â ¹°¿¡ Àß ³ìÁö ¾Ê°í ´Ü¹éÁú°ú ¼ºÁúÀÌ ºñ½ÁÇÏ´Ù. ³úÇϼöüȣ¸£¸ó, ºê¶óµðŰ´Ñ µî°ú °°ÀÌ »ý¸®Àû±â´ÉÀÌ ÇöÀúÇÑ °ÍÀº »ý¸®È°¼ºÆéƼµå(bioactive peptide)¶ó°í ÇÑ´Ù. |
||
| ECG | Electro-Cardio-Graphy(-Gram); ½ÉÀüµµ = EKG 1. Conducting System Structu... |
|---|---|
| JVP | [POMD P 49 - 52] 1) Jugular Vein Pressure 2) Jugular Venous Pulse ... |
| AT III | angiotensin III; antithrombin III |
| PCP | parachlorophenate; patient care plan; pentachlorophenol; 1-(1-phenylcyclohexyl)piperidine; periphera... |
| ML | I, II, III, IV mucolipidosis I, II, III, IV |
| PIIINP | Procollagen type III aminoterminal peptide |
|---|---|
| PIIIP | Type III procollagen peptide |
| PIIINP | N-propeptide of type III procollagen |
| P IIIP | Type III procollagen |
| CTAP III | Connective tissue activating peptide III |
pseudounipolar bipolar III disorder
transverse facial vein
corticotropin-releasing factor (ºÎ½Å ÇÇÁú È£¸£¸ó À¯¸® ¿ä¼Ò, ºÎ½Å ÇÇÁú È£¸£¸ó À¯¸® ÀÎÀÚ
| connective tissue activating peptide III | Cytokine, produced from platelet basic protein, that acts as a growth factor. (18 Nov 1997) |
|---|---|
| procollagen | <cell biology> Triple helical trimer of collagen molecules in which the terminal extension peptides are linked by disulphide bridges, the terminal peptides are later removed by specific proteases to produce a tropocollagen molecule. (18 Nov 1997) |
| procollagen aminoproteinase | An extracellular enzyme that participates in the processing of collagen, removing the extension peptide at the amino-terminal end of procollagen. (05 Mar 2000) |
| procollagen carboxyproteinase | An extracellular enzyme that participates in the processing of collagen, removing the extension peptide at the carboxy-terminal end of procollagen. (05 Mar 2000) |
| procollagen C-endopeptidase | <enzyme> Cleaves the carboxyl-terminal propeptides from type I pr; in 1996 determined to be identical to bone morphogenetic protein 1 Registry number: EC 3.4.24.19 Synonym: procollagen c-protease, type I procollagen carboxyl-terminal proteinase, c-proteinase, procollagen, procollagen endopeptidase (carboxy terminal splitting), procollagen c-proteinase, bone morphogenetic protein 1, bone morphogenic protein 1, bmp-1 (26 Jun 1999) |
| procollagen-lysine, 2-oxoglutarate 5-dioxygenase | <enzyme> A mixed-function oxygenase that catalyses the hydroxylation of peptidyllysine, usually in protocollagen, to peptidylhydroxylysine. The enzyme utilises molecular oxygen with concomitant oxidative decarboxylation of the cosubstrate 2-oxoglutarate to succinate. Chemical name: Procollagen-L-lysine,2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating) Registry number: EC 1.14.11.4 (12 Dec 1998) |
| procollagen n-endopeptidase | <enzyme> An extracellular endopeptidase which excises a block of peptides at the amino terminal, nonhelical region of the procollagen molecule with the formation of collagen. Absence or deficiency of the enzyme causes accumulation of procollagen which results in the inherited connective tissue disorder--dermatosparaxis. Registry number: EC 3.4.24.14 (12 Dec 1998) |
| procollagen peptidase | <enzyme> The proteases that remove the terminal extension peptides of procollagen, deficiency of these enzymes leads to dermatosparaxis or Ehlers Danlos syndrome. (18 Nov 1997) |
| procollagen-proline dioxygenase | <enzyme> A mixed-function oxygenase that catalyses the hydroxylation of a prolyl-glycyl-containing-peptide, usually in protocollagen, to a hydroxyprolylglycyl-containing-peptide. The enzyme utilises molecular oxygen with a concomitant oxidative decarboxylation of 2-oxoglutarate to succinate. Chemical name: Procollagen-L-proline,2-oxoglutarate:oxygen oxidoreductase Registry number: EC 1.14.11.2 (12 Dec 1998) |
| angiotensin III | <chemical> A heptapeptide formed by the enzymatic hydrolysis of angiotensin II. It has greater activity than angiotensin II for stimulating aldosterone synthesis and in the release of prostaglandins but only 20% of the pressor activity. Chemical name: Angiotensin II, 1-de-L-aspartic acid- (12 Dec 1998) |
| annexin III | <enzyme> A protein of the annexin family that catalyses the conversion of 1-d-inositol 1,2-cyclic phosphate and water to 1-d-myo-inositol 1-phosphate. Chemical name: 1-D-myo-Inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase Registry number: EC 3.1.4.36 (12 Dec 1998) |
| antithrombin III | <haematology> Antithrombin III is a protein which stimulates the removal of blood clots in the bloodstream. Small blood clots form normally within the bloodstream, but are normally dissolved via the bodys antithrombin III. Conditions that may have an associated low value of antithrombin III include: liver disease and DIC. Normal values are: 0.20 to 0.45 mg/ml or more than 50% of the laboratory control value. Conditions where there is a deficiency of this important protease inhibitor can result in a condition of hypercoagulation, resulting in an increased risk for blood clot formation. Inheritance: autosomal dominant. (13 Jan 1998) |
| apolipoprotein C-III | <biochemistry> An apolipoprotein found in VLDL, HDL, and chylomicrons. (05 Mar 2000) |
| arsenazo III | <chemical> Metallochrome indicator that changes colour when complexed to the calcium ion under physiological conditions. It is used to measure local calcium ion concentrations in vivo. Pharmacological action: dyes, indicators and reagents. Chemical name: 2,7-Naphthalenedisulfonic acid, 3,6-bis((2-arsonophenyl)azo)-4,5-dihydroxy- (12 Dec 1998) |
| arteriae intercostales posteriores III-XI | posterior intercostal arteries 3-11 |
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