| ¿µ¹® | oral administration | ÇÑ±Û | °æ±¸º¹¿ë |
|---|---|---|---|
| ¼³¸í | ¾àÀ» Åõ¿©ÇÏ´Â ¹æ¹ý¿¡´Â ¿©·¯ °¡Áö°¡ ÀÖ´Ù. Å©°Ô ³ª´©¾î º¸¸é, ÀÔÀ» °ÅÃÄ À§Ã¢Àڰ踦 ÅëÇØ ³Ö´Â ¹æ¹ý°ú À§Ã¢Àڰ踦 ÅëÇÏÁö ¾Ê°í ¹Ù·Î Ç÷¾×À¸·Î ³Ö´Â ¹æ¹ýÀÌ ÀÖ´Ù. À§Ã¢Àڰ踦 ÅëÇÏÁö ¾Ê´Â ¹æ¹ýÀ¸·Î °¡Àå ÈçÇÑ ¹æ¹ýÀº Áֻ縦 ÀÌ¿ëÇÏ´Â ¹æ¹ýÀÌ´Ù. ÇÏÁö¸¸, À̿ܿ¡ Ç×¹®À» ÅëÇØ ³Ö´Â Á¾à½Ä¹æ¹ý°ú Çô¹Ø¿¡ ³Ö´Â Çô¹ØÅõ¿©¹ýµµ ÀÖ´Ù. ±×·¯³ª ´ëºÎºÐÀÇ ¾àÁ¦´Â °æ±¸º¹¿ëÀ» ÇÏ°Ô µÈ´Ù. °æ±¸º¹¿ë¿¡ ´ëÇÑ ¾àÀÚ´Â p.o.(per oral)·Î Ç¥±âÇÑ´Ù. °æ±¸º¹¿ëÁ¦ÀÇ ´ÜÁ¡Àº º¹¿ëÇÑ ¾àÁ¦°¡ À§Ã¢ÀÚ°ü°è¸¦ °ÅÄ¡¸é¼ »ç¶÷¸¶´Ù °¢±â ´Ù¸¥ Èí¼öÁ¤µµ¿Í ´ë»çÁ¤µµ¸¦ °ÅÄ¡°Ô µÇ¹Ç·Î ÀÏÁ¤ÇÑ ³óµµÀ¯Áö°¡ ¾î·Æ´Ù´Âµ¥ ÀÖ´Ù. ¶ÇÇÑ °æ±¸º¹¿ëÁ¦ÀÇ ¸ð¾çÀÌ Ä¸½¶ÇüÀÎÁö, ȤÀº °¡·çÇüÀÎÁö¿¡ µû¶ó¼µµ °°Àº ¾àÀÌÁö¸¸, ¼·Î ´Ù¸¥ È¿°ú¸¦ ³ªÅ¸³¾ ¼ö ÀÖ´Ù. |
||
| ¿µ¹® | oral cavity | ÇÑ±Û | ±¸° |
|---|---|---|---|
| ¼³¸í | ÀÔÀ» ¹ú¿©¼ ÀÔ¼Ó¿¡¼ º¼ ¼ö ÀÖ´Â °ø°£À¸·Î ÀÔõÀå, Æíµµ, ¸ñÁ¥À» º¼ ¼ö ÀÖ´Ù. ![]() |
||
| ¿µ¹® | oral cavity | ÇÑ±Û | ÀÔ¾È |
|---|---|---|---|
| ¼³¸í | ÀÔÀ» ¹ú¿©¼ ÀÔ¼Ó¿¡¼ º¼ ¼ö ÀÖ´Â °ø°£À¸·Î ÀÔõÀå, Æíµµ, ¸ñÁ¥À» º¼ ¼ö ÀÖ´Ù. |
||
| ORS | olfactory reference syndrome; oral rehydration solution; oral surgery, oral surgeon; Orthopaedic Res... |
|---|---|
| OCP | octacalcium phosphate; ocular cicatricial pemphigoid; oral case presentation; oral contraceptive pil... |
| OET | oral endotracheal tube; oral esophageal tube |
| OHI | Occupational Health Institute; operative hypertension indicator; oral hygiene index; Oral Hygiene In... |
| APRP | acidic proline-rich protein; acute phase reactant protein |
| DHP | 3,4,dehydro-D,L-proline |
|---|---|
| PRO | L-proline |
| PRP | Proline-Rich Polypeptides |
| PDPK | Proline-directed protein kinase |
| PYK2 | Proline-rich Tyrosine Kinase-2 |
naso-oral
| 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) |
|---|---|
| proline | <amino acid> One of the 20 amino acids directly coded for in proteins. Structure differs from all the others, in that its side chain is bonded to the nitrogen of the _ amino group, as well as the _ carbon. This makes the amino group a secondary amine and so proline is described as an imino acid. Has strong influence on secondary structure of proteins and is much more abundant in collagens than in other proteins, occurring especially in the sequence glycine proline hydroxyproline. A proline rich region seems to characterise the binding site of SH3 domains. (18 Nov 1997) |
| proline, 2-oxoglutarate 3-dioxygenase | <enzyme> Prolyl 3-hydroxylase is separate enzyme from prolyl 4-hydroxylase; catalyses post translational modification of collagen Registry number: EC 1.14.11.7 Synonym: proline 3-hydroxylase, prolyl 3-hydroxylase (26 Jun 1999) |
| proline aminopeptidase | A hydrolase cleaving l-proline residues from the N-terminal position in peptides. Synonym: proline aminopeptidase. (05 Mar 2000) |
| proline-beta-naphthylamidase | <enzyme> From pig intestinal mucosa; hydrolyzes proline-beta-naphthylamidase; distinct from proline aminopeptidase; inhibited by active site serine-specific protease inhibitors Registry number: EC 3.4.11.- Synonym: pro-naphthylamidase (26 Jun 1999) |
| proline dehydrogenase | An oxidoreductase reducing 1-pyrroline-2-carboxylate to l-proline with NAD(P)H. Synonym: proline dehydrogenase, proline oxidase. (05 Mar 2000) |
| proline dipeptidase | <enzyme> An enzyme cleaving aminoacyl-l-proline bonds in dipeptides containing a C-terminal prolyl residue; a deficiency of this enzyme results in hyperimidodipeptiduria. Synonym: imidodipeptidase, peptidase D, prolidase. (05 Mar 2000) |
| proline iminopeptidase | A hydrolase cleaving l-proline residues from the N-terminal position in peptides. Synonym: proline aminopeptidase. (05 Mar 2000) |
| proline oxidase | <enzyme> The first enzyme of the proline degradative pathway. It catalyses the oxidation of proline to pyrroline-5-carboxylic acid in the presence of oxygen and water. The action is not reversible. The specific activity of proline oxidase increases with age. Registry number: EC 1.5.3.- (12 Dec 1998) |
| proline permease | <chemical> Prnb isolated from aspergillus nidulans Chemical name: permease, proline Synonym: l-proline permease, proline porter, proline transporter, putp gene product, sodium-proline permease, na(+)-proline permease, prnb gene product (26 Jun 1999) |
| proline racemase | <enzyme> An enzyme that reversibly converts d-proline to l-proline. (05 Mar 2000) |
| proline-specific dipeptidylcarboxypeptidase | <enzyme> From streptomyces species; removes diproline form c-terminus of proline-containing peptides such as boc-pro-pro-pro-pro or leu-pro-pro-pro-pro-pro Registry number: EC 3.4.15.- Synonym: pro-dpp-carboxypeptidase (26 Jun 1999) |
| protein-proline kinase | <enzyme> Phosphorylates synapsin i; phosphorylation takes place on serine 20, which is flanked by two proline molecules; heterodimer of p34(cdc2)/p58(cyclin a) Registry number: EC 2.7.10.- Synonym: proline-directed protein kinase (26 Jun 1999) |
| SH3 domain-containing proline-rich kinase | <enzyme> A protein kinase which both phosphorylates ser and thr residues and has an sh3 domain; contains 847 amino acid residues; mol mass 92,688 da; genbank u07747 Registry number: EC 2.7.10.- Synonym: src-homology 3 domain-containing proline-rich kinase, sprk protein, sprk gene product (26 Jun 1999) |
| d-proline reductase | An oxidoreductase reversibly reacting d-proline with NADH to produce 5-aminovalerate and NAD+. (05 Mar 2000) |
Á¦Ç°¸í |
ÆÇ¸Å»ç |
º¸ÇèÄÚµå | ¼ººÐ/ÇÔ·® | ±¸ºÐ/º¸Çè±Þ¿© |
|---|
Á¦Ç°¸í |
ÆÇ¸Å»ç |
º¸ÇèÄÚµå | ¼ººÐ/ÇÔ·® | ±¸ºÐ/º¸Çè±Þ¿© |
|---|