| ¿µ¹® | streptococcus | ÇÑ±Û | »ç½½¾Ë±Õ, ¿¬¼â»ó±¸±Õ |
|---|---|---|---|
| ¼³¸í | ±×¶÷¾ç¼º±¸±ÕÀ¸·Î ¹è¾ç½Ã ½ÖÀ̳ª ÁÙÀ» Çü¼ºÇÏ´Â °ÍÀÌ Æ¯Â¡ÀÌ´Ù. »ç½½¾Ë±Õ¼Ó¿¡´Â 20¿© °³ÀÇ Á¾ÀÌ Æ÷ÇԵǴµ¥ S. pyogenes(group A), S. agalactiae(group B), enterococcus(group D)¿Í °ú°Å¿¡ µû·Î ºÐ·ùµÇ¾ú´ø S. pneumoniae°¡ Áß¿äÇÏ´Ù. |
||
| Sf | Streptococcus faecalis |
|---|---|
| MMP | matrix metalloproteinase; muscle mechanical power |
| MMPI | matrix metalloproteinase specific for collagen type I; Minnesota Multiphasic Personality Inventory |
| PUMP | putative metalloproteinase |
| GBS | 1) Guillain-Barr Syndrome = PIP; Post-Infectious Polyneuropat... |
| GAS | Group A Streptococcus |
|---|---|
| GABHS | Group A beta haemolytic streptococcus |
| GBS | Group B Streptococcus |
| GBS | Group B beta--hemolytic streptococcus |
| PRSP | Penicillin-resistant Streptococcus pneumoniae |
| Streptococcus faecalis metalloproteinase | <enzyme> Bacterial metalloproteinase from streptococcus faecalis Registry number: EC 3.4.24.- Synonym: streptococcus faecalis metalloendopeptidase, metalloproteinase (streptococcus faecalis), sf-metalloproteinase (26 Jun 1999) |
|---|
| Streptococcus faecalis | A species found in human faeces and in the intestines of many warm-blooded animals; occasionally found in urinary infections and in blood and heart lesions in cases of subacute endocarditis; associated with European foul brood of bees and with mild outbreaks of food poisoning. (05 Mar 2000) |
|---|---|
| enterococcus faecalis | A species of gram-positive, coccoid bacteria commonly isolated from clinical specimens and the human intestinal tract. most strains are nonhemolytic. (12 Dec 1998) |
| Aspergillus fumigatus metalloproteinase | <enzyme> Mol mass 82 kD; pi 5.6; hydrolyzes phenylazobenzyloxycarbonyl-pro-leu-gly-pro-arg and cleaves native rat type I collagen Registry number: EC 3.4.24.- Synonym: a. Fumigatus metalloproteinase, af-mep (26 Jun 1999) |
| BaP1 metalloproteinase | <enzyme> From bothrops asper venom; causes haemorrhage at site of venom injection and systemically in different organs Registry number: EC 3.4.24.- (26 Jun 1999) |
| membrane-type 3 matrix metalloproteinase | <enzyme> Sm3 is a soluble form of mt3-mmp, probably an alternatively sliced variant. Registry number: EC 3.4.24.- Synonym: mt3-mmp, sm3-mmp (26 Jun 1999) |
| membrane-type 4 matrix metalloproteinase | <enzyme> Cloned from breast carcinoma. Registry number: EC 3.4.24.- Synonym: mt4-mmp, mmp-17 gene product, mmp-17 (26 Jun 1999) |
| membrane-type matrix metalloproteinase | <enzyme> Activates gelatinase a; isolated from a human placenta cdna gene library; contains a transmembrane domain; do not use for any other numbered matrix metalloproteinases; genbank d26512 Registry number: EC 3.4.24.- Synonym: mt-mmp, mmp-x1 protein, matrix metalloproteinase, membrane-type, mmp14 gene product, mmp-14 gene product, mt1-mmp, matrix metalloproteinase 14, mt2-mmp, mmp15 gene product, mmp16 gene product (26 Jun 1999) |
| haemorrhagic metalloproteinase | <enzyme> Extracted from vipera berus berus venom; hydrolyzes casein, fibrinogen and splits the insulin b chain at positions ala(14)-leu(15), tyr(16)-leu(17), his(10)-leu(11); digests alpha chain of fibrinogen Registry number: EC 3.4.24.- (26 Jun 1999) |
| Xolloid metalloproteinase | <enzyme> Tolloid-like protein from xenopus with development-regulating activity; acts as a ventralizing agent that mimics low doses of bone morphogenetic protein-4 Registry number: EC 3.4.24.- Synonym: xolloid gene product (26 Jun 1999) |
| S. marcescens minor metalloproteinase | <enzyme> Precursor protein consists of 352 amino acids, mw 38.479 kD from serratia marcescens; mature protein consists of 300 amino acids mw 32.515 kD with optimal activity at pH 8.0 and 50c; do not confuse with smp protein, a membrane protein from E coli Registry number: EC 3.4.24.- Synonym: smp proteinase (26 Jun 1999) |
| tissue-inhibitor of metalloproteinase-1 | <chemical> A member of the family of tissue inhibitor of metalloproteinases. It is a n-glycosylated protein, molecular weight 28 kD, produced by a vast range of cell types and found in a variety of tissues and body fluids. It has been shown to suppress metastasis and inhibit tumour invasion in vitro. Pharmacological action: antineoplastic agent, protease inhibitors. (12 Dec 1998) |
| tissue inhibitor-of metalloproteinase-2 | <chemical> A member of the family of tissue inhibitor of metalloproteinases. It is a 21 kD nonglycosylated protein found in tissue fluid and is secreted as a complex with progelatinase a by human fibroblast and uncomplexed from alveolar macrophages. An overexpression of timp-2 has been shown to inhibit invasive and metastatic activity of tumour cells and decrease tumour growth in vivo. Pharmacological action: antineoplastic agent, protease inhibitors. (12 Dec 1998) |
| tissue inhibitor of-metalloproteinase-3 | <chemical> A member of the family of tissue inhibitor of metalloproteinases. It is a 21 kD, nonglycosylated protein. Timp-3 does not show a high degree of structural similarity unlike timp-1 and timp-2 which are structurally similar. However, it does possess a high degree of structural similarity with that of chicken timp-3 (chimp-3). Human timp-3 is of particular concern because of its potential role in cancer, arthritis, and eye diseases. Pharmacological action: antineoplastic agent, protease inhibitors. (12 Dec 1998) |
| tissue inhibitors of metalloproteinase | <cell biology> Family of proteins of around 200 residues that can inhibit metalloproteinases, for example collagenase, by binding to them. (18 Nov 1997) |
| Streptococcus | <bacteria, organism> A genus of bacteria that are gram-positive cocci, often occurring in chains of varying length. Some pathogenic species produce exotoxins. In man, streptococcal species are responsible for numerous infections such as scarlet fever, tonsillitis, erysipelas (skin infection), endocarditis, rheumatic fever, glomerulonephritis, impetigo, pneumonia, meningitis, pharyngitis, lymphadenitis and wound infections. Streptococcus pneumoniae is the main culprit in lobar and bronchopneumonia. Streptococci have anti-phagocytic components (hyaluronic acid rich capsule and M protein) and release various toxins streptolysins O and s, erythrogenic toxin) and enzymes streptokinase, streptodornase, hyaluronidase and proteinase. Haemolytic streptococci (viridans streptococci) produce limited haemolysis on blood agar, include Streptococcus mutans, Streptococcus salivarius and Streptococcus pneumoniae. Beta haemolytic streptococci, of which Streptococcus pyogenes is the only species, though there are many serotypes, produce a broad zone of almost complete haemolysis on blood agar as a result of streptolysin O and S release. Alpha streptococci are nonhaemolytic (e.g. Streptococcus faecalis). (30 Sep 1997) |
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¿© |
|---|