| Sm | samarium; Serratia marcescens, Smith [antigen] |
|---|
| MNase | Micrococcal nuclease |
|---|---|
| SNase | Staphylococcal Nuclease |
| Nase | nuclease |
| Serratia marcescens nuclease | <enzyme> Formerly EC 3.1.4.9; acts on DNA, RNA and double-stranded homopolymers such as poly i-c; has been sequenced, genbank m19495 Registry number: EC 3.1.30.2 Synonym: nucleate endonuclease, nuclease o, endonuclease (serratia marcescens), nuclease sm, nuclease sm1, nuclease sm2, extracellular nuclease, serratia marcescens (26 Jun 1999) |
|---|
| Serratia marcescens | A gram-negative bacterium that is very common in soil and water, most strains produce a characteristic pigment, prodigiosin. Opportunistic human pathogens, infecting mainly hospital patients. (18 Nov 1997) |
|---|---|
| endonuclease Serratia marcescens | A nuclease (a nucleate oligonucleotidohydrolase) that forms oligonucleotides ending in 5'-phosphates from RNA and DNA; hydrolyzes both double-stranded and single-stranded polynucleic acids. Synonym: nucleate endonuclease. (05 Mar 2000) |
| 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) |
| serratia | A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that occurs in the natural environment (soil, water, and plant surfaces) or as an opportunistic human pathogen. (12 Dec 1998) |
| serratia infections | Infections with bacteria of the genus serratia. (12 Dec 1998) |
| 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) |
| S1 nuclease mapping | A method for locating the 5' end of a transcript in a mixture of RNA. (05 Mar 2000) |
| 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) |
| sugar-non-specific nuclease | <enzyme> An exocytoplasmic sugar-non-specific nuclease that is able to degrade linear or covalently closed circular double-stranded DNA as well as single-stranded DNA or RNA; from cyanobacterium anabaena; mw 29 kD; amino acid sequence has been determined Registry number: EC 3.1.- Synonym: nuca gene product, anabaena (26 Jun 1999) |
제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
|---|
제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
|---|