| 영문 | Dilatation and Curettage(D & C) | 한글 | 자궁긁어냄술, 자궁목확장 |
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| 설명 | 자궁이란 태아가 수태되어서 분만전까지 발육하고 성장하는 공간이다. 자궁속에 병변이 있어 임신이 계속될 수 없거나 아니면 다른 이유로 임신되어 있는 태아를 제거하고자 할 경우에 사용되는 방법이다. 여기서 긁어내기 위하여는 우선 자궁의 입구에 해당하는 자궁목을 확장시켜야 한다. 여기에는 급속히 확장을 시도하는 법과 서서히 확장을 시도하는 2가지 방법이 있다. 자궁목을 급속히 확장할 때는 헤가르 목관확장기(Hegar's dilatator)를 사용한다. 이것은 작은 금속막대로 작은 크기부터 큰 크기까지 다양한 크기가 있어서 우선 작은 막대로 시작하여 점점 큰 크기의 막대를 자궁목에 넣어서 자궁목을 확장시킨다. 서서히 확장시킬 때는 Laminaria tent를 목관에 삽입하는 방법을 사용한다. Laminaria tent란 해초로 만든 작은 막대로 수분을 흡수하면 점점 늘어나는 성질이 있다. 이것을 자궁의 목에 넣으면 이것이 수분을 흡수하여 늘어나므로 천천히 자궁의 목이 늘어난다. 자궁목이 충분히 늘어나면 그 속으로 끝이 숟가락처럼 생긴 기구를 넣어서 자궁속의 병변이나 임신된 태아를 긁어내는데 여기에 사용되는 숟가락처럼 생긴 기구를 큐렛이라고 한다. 초기 임신중절 즉 유산과 같은 임신과 관련된 경우뿐만 아니라, 비임신 자궁의 자궁내막조직의 채취 및 제거를 위해서도 행해지는 수기이다. 이는 원칙적으로 마취하에 실시되는 것으로 자궁목관을 확장하고 기구로 자궁 내용물을 제거하고 큐렛으로 자궁내벽을 깨끗이 한다. 자궁천공이나 자궁목의 파열 등의 위험이 따르며, 수술후 감염 또는 출혈 등에 대한 주의가 필요하다. |
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| PEP | peptidase; phospho(enol)pyruvate; peer evaluation program; phosphoenolpyruvate; pigmentation, edema,... |
|---|---|
| LAP | 1) Leukocyte Alkaline Phosphatase 2) Leucine Amino-Peptidase |
| Pep | peptidase |
| PEPA | peptidase A |
| PEPB | peptidase B |
| NTI | Non-thyroidal illness |
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| DP IV | Dipeptidyl Peptidase IV |
| DPP IV | Dipeptidyl Peptidase IV |
| DPP | Dipeptidyl peptidase |
| DPPI | Dipeptidyl peptidase I |
acute angle
| thyroidal articular surface of cricoid | One of two small circular facets on the lateral surface of the cricoid cartilage near the inferior margin of the junction of the arch and lamina for articulation with the inferior horns of the thyroid cartilage. Synonym: facies articularis thyroidea cricoideae. (05 Mar 2000) |
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| alkaline D-peptidase | <enzyme> A penicillin-recognizing enzyme from bacillus cereus; has beta-lactamase activity; genbank d86380 Registry number: EC 3.4.99.- Synonym: ADP gene product, alkaline d-stereospecific endopeptidase (26 Jun 1999) |
| aspartyllysine peptidase | <enzyme> From human intestinal brush border; stabilised by zn+2 Registry number: EC 3.4.13.- Synonym: zn-stable aspartyllysine peptidase (26 Jun 1999) |
| C5a peptidase | <enzyme> Streptococcus pyogenes enzyme inactivates complement 5a by cleaving at lysine 68, removing a six-amino acid fragment Pharmacological action: complement inactivators Registry number: EC 3.4.99.- Synonym: streptococcus c5a peptidase, gbs c5a-ase, group b streptococci c5a-ase, scpa protein (26 Jun 1999) |
| matrix processing peptidase | <enzyme> From matrix fraction of rat liver mitochondria; cleaves mitochondrial protein precursors; inhibited by metal chelators and reactived by mn2+; classified as EC 3.4.24.64 Registry number: EC 3.4.24.- Synonym: mitochondrial processing peptidase, mitochondrial processing protease, alpha-mpp, beta-mpp, p-52 protein, rat, p-55 protein, rat, mas1 protein, yeast, mas2 protein, yeast (26 Jun 1999) |
| peptidase | <enzyme> Alternative name for a protease. (18 Nov 1997) |
| peptidase D | <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) |
| peptidase P | <enzyme> A hydrolase cleaving C-terminal dipeptides from a variety of substrates, including angiotensin I, which is converted to angiotensin II and histidylleucine. An important step in the metabolism of certain vasopressor agents. It is a chloride-dependent, zinc glycoprotein that is generally membrane-bound and active at neutral pH. Only single dipeptides are released from angiotensin I and bradykinin because of the lack of activity on bonds involving proline. It may also have endopeptidase activity on some substrates. Registry number: EC 3.4.15.1 Synonym: carboxycathepsin, dipeptidyl carboxypeptidase, kinase II, peptidase P. (22 Sep 2002) |
| mitochondrial intermediate peptidase | <enzyme> Removes the octapeptide from the amino terminus of the intermediate protein processed from the protein precursor of certain mitochondrial proteins by the mitochondrial processing peptidase; smip from schizophyllum commune; rmip from rat; ymip from saccharomyces cerevisiae Registry number: EC 3.4.24.59 Synonym: mip peptidase, smip peptidase, rmip peptidase, ymip peptidase (26 Jun 1999) |
| 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) |
| pyroglutamyl-peptidase I | <enzyme> An enzyme that catalyses the release of a n-terminal pyroglutamyl group from a polypeptide provided the next residue is not proline. It is inhibited by thiol-blocking reagents and occurs in mammalian tissues, microorganisms, and plants. Registry number: EC 3.4.19.3 (12 Dec 1998) |
| PZ-PLGPA peptidase | <enzyme> Endopeptidase from treponema denticola Registry number: EC 3.4.21.- (26 Jun 1999) |
| signal peptidase | A peptide present on proteins that are destined either to be secreted or to be membrane components. It is usually at the N terminus and normally absent from the mature protein. Normally refers to the sequence (ca 20 amino acids) that interacts with signal recognition particle and directs the ribosome to the endoplasmic reticulum where co translational insertion takes place. Could also refer to sequences that direct post translational uptake by organelles. Signal peptides are highly hydrophobic but with some positively charged residues. The signal sequence is normally removed from the growing peptide chain by signal peptidase, a specific protease located on the cisternal face of the endoplasmic reticulum. See: signal recognition particle. (18 Nov 1997) |
| signal peptidase complex | A peptide present on proteins that are destined either to be secreted or to be membrane components. It is usually at the N terminus and normally absent from the mature protein. Normally refers to the sequence (ca 20 amino acids) that interacts with signal recognition particle and directs the ribosome to the endoplasmic reticulum where co translational insertion takes place. Could also refer to sequences that direct post translational uptake by organelles. Signal peptides are highly hydrophobic but with some positively charged residues. The signal sequence is normally removed from the growing peptide chain by signal peptidase, a specific protease located on the cisternal face of the endoplasmic reticulum. See: signal recognition particle. (18 Nov 1997) |
| N-acetylaspartylglutamate peptidase | <enzyme> Produces glutamate plus n-acetylaspartate; found throughout rat CNS Registry number: EC 3.4.13.- Synonym: naag peptidase (26 Jun 1999) |
제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
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제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
|---|