| APSGN | Acute Post-Streptococcal Glomerulo-Nephritis; ¿¬¼â»ó ±¸±Õ°¨¿°ÈÄ ±Þ¼º »ç±¸Ã¼ ½Å¿° |
|---|---|
| PSGN | Post-Streptococcal Glomerulo-Nephritis |
| EOGBS | early onset group B streptococcal [infection] |
| GRABS | group A beta-hemolytic streptococcal pharyngitis |
| ISCW | immunosuppression of streptococcal wall [antigen] |
| MNase | Micrococcal nuclease |
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| SNase | Staphylococcal Nuclease |
| Nase | nuclease |
| GAS | Group A Streptococcal |
| GABHS | Group A beta hemolytic streptococcal |
| streptococcal nuclease | <enzyme> From streptococcus haemolyticus; degrades RNA and DNA producing oligonucleotides terminating in 5'-phosphate Registry number: EC 3.1.30.- (26 Jun 1999) |
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| acute post-streptococcal glomerulonephritis | <nephrology> A disease of the kidneys that results in inflammation of the glomerulus (the portion of the kidney that filters the blood). Conditions which may cause glomerulonephritis include post-streptococcal disease (strep throat), lupus, syphilis, bacterial endocarditis, membranoproliferative glomerulonephritis, sepsis, vasculitis, Goodpasture's syndrome, typhoid fever, Henoch-Schonlein purpura, hepatitis or a viral infection (for example mumps, measles, mononucleosis). (27 Sep 1997) |
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| group A streptococcal necrotizing fasciitis | A complication of infection with GAS (group A streptococci) in which the bacteria attacks and destroys muscle tissue. According to the CDC, 5-10% of people with severe GAS infection develop necrotizing fasciitis. Though the infection can be treated with antibiotics, the fatality rate is close to 30%. This complication often develops as a wound infection after surgery or injury. (05 Mar 2000) |
| streptococcal | Relating to or caused by any organism of the genus Streptococcus. (05 Mar 2000) |
| streptococcal fibrinolysin | <enzyme> Plasminogen activator released by Streptococcus pyogenes. Occurs in two forms, A and B. (18 Nov 1997) |
| streptococcal infections | Infections with bacteria of the genus streptococcus. (12 Dec 1998) |
| streptococcal lymphadenitis | A contagious bacterial disease of pigs caused by a group E streptococcus and characterised by the formation of abscesses in the cervical and/or cephalic lymph nodes. (05 Mar 2000) |
| streptococcal pneumonia | Pneumonia due to Streptococcus pyogenes. (05 Mar 2000) |
| streptococcal toxins | Group of haemolytic exotoxins released by Streptococci. _ haemolysin: 26-39 Kd (four types), forms ring like structures in membranes (see Streptolysin O). Lipid target unclear. _ haemolysin: a hot cold haemolysin with sphingomyelinase C activity. _ haemolysin: complex of two proteins (29 and 26 kD) that act synergistically, rabbit erythrocytes particularly sensitive. _ toxin: heat stable peptide (5 kD) with high proportion of hydrophobic amino acids. Seems to act in a detergent like manner (c.f. Subtilysin), but may form hydrophilic transmembrane pores by cooperative interaction with other _ toxin molecules. Leucocidin (Panton Valentine leucocidin): two components f (fast migration on CM cellulose column: 32 kD) and s (slow: 38 kD). Mode of action contentious. See: Streptococcus, streptolysins O and S, erythrogenic toxin. (18 Nov 1997) |
| APEX nuclease | <enzyme> DNA repair enzyme having both exonuclease and apurinic-apyrimidinic endonuclease activities; apex is from mouse; rapen from rat has high homology with apex Registry number: EC 3.1.- Synonym: rapen redox factor (26 Jun 1999) |
| aspergillus nuclease s1 | <enzyme> An enzyme that catalyses endonucleolytic cleavage to 5-phosphomononucleotides and 5-phosphooligonucleotide end-products. It has a preference for single-stranded substrates but is active with either ribo- or deoxyribonucleic acids. Registry number: EC 3.1.30.1 (12 Dec 1998) |
| viral alkaline nuclease | <enzyme> Has both exo and endonuclease activity Registry number: EC 3.1.- Synonym: hsv type 1 alkaline nuclease, herpes simplex virus type I alkaline nuclease, alkaline nuclease, herpes simplex virus (26 Jun 1999) |
| repair nuclease | <enzyme, molecular biology> Class of enzymes involved in DNA repair. It includes endonucleases that recognise a site of damage or an incorrect base pairing and cut it out and exonucleases that remove neighbouring nucleotides on one strand. These are then replaced by a DNA polymerase. (18 Nov 1997) |
| restriction nuclease | <enzyme, molecular biology> Class of bacterial enzymes that cut DNA at specific sites. In bacteria their function is to destroy foreign DNA, such as that of bacteriophages (host DNA is specifically modified at these sites). Type I restriction endonucleases occur as a complex with the methylase and a polypeptide that binds to the recognition site on DNA. They are often not very specific and cut at a remote site. Type II restriction endonucleases are the classic experimental tools. They have very specific recognition and cutting sites. The recognition sites are short, 4-8 nucleotides and are usually palindromic sequences. Because both strands have the same sequence running in opposite directions the enzymes make double stranded breaks, which, if the site of cleavage is off centre, generates fragments with short single stranded tails, these can hybridise to the tails of other fragments and are called sticky ends. They are generally named according to the bacterium from which they were isolated (first letter of genus name and the first two letters of the specific name). The bacterial strain is identified next and multiple enzymes are given Roman numerals. For example the two enzymes isolated from the R strain of E. Coli are designated Eco RI and Eco RII. (10 Mar 1998) |
| micrococcal nuclease | <enzyme> An enzyme that catalyses the endonucleolytic cleavage to 3'-phosphomononucleotide and 3'-phospholigonucleotide end-products. It can cause hydrolysis of double- or single-stranded DNA or RNA. Registry number: EC 3.1.31.1 (12 Dec 1998) |
| mung bean nuclease | Endonuclease S1 (Aspergillus). (05 Mar 2000) |
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