| 序号 | 专利名 | 申请号 | 申请日 | 公开（公告）号 | 公开（公告）日 | 发明人 |
|---|---|---|---|---|---|---|
| 1 | Soluble and stable human 5-lipoxygenase | US13700507 | 2011-05-31 | US08877476B2 | 2014-11-04 | Marcia E. Newcomer; Sue G. Bartlett; Nathaniel C. Gilbert |
| A soluble and stable form of 5-lipoxygenase (5-LOX) has been made, 5-Lox is the enzyme which initiates leukotriene biosynthesis by catalyzing the two-step transformation of arachidomc acid to leukotriene A4 (LTA4). The soluble and stable 5-LOX is suitable for a number of applications, including, but not limited to, high throughput screening of 5-LOX inhibitors, structural analysis of the enzyme's active site, designing inhibitors based on the three-dimensional structure of the enzyme's active site, and synthesis of LTA4. Using Stable-5-LOX, the crystal structure for 5-LOX has been resolved and the amino acids defining the active site determined. | ||||||
| 2 | A Soluble and Stable Human 5-Lipoxygenase | US13700507 | 2011-05-31 | US20130210052A1 | 2013-08-15 | Marcia E. Newcomer; Sue G. Bartlett; Nathaniel C. Gilbert |
| A soluble and stable form of 5-lipoxygenase (5-LOX) has been made, 5-Lox is the enzyme which initiates leukotriene biosynthesis by catalyzing the two-step transformation of arachidomc acid to leukotriene A4 (LTA4). The soluble and stable 5-LOX is suitable for a number of applications, including, but not limited to, high throughput screening of 5-LOX inhibitors, structural analysis of the enzyme's active site, designing inhibitors based on the three-dimensional structure of the enzyme's active site, and synthesis of LTA4. Using Stable-5-LOX, the crystal structure for 5-LOX has been resolved and the amino acids defining the active site determined. | ||||||
| 3 | Production of human 5-lipoxygenase | JP4020689 | 1989-02-22 | JPH02219570A | 1990-09-03 | MATSUMOTO TAKASHI; NOGUCHI MASATO; NAKAMURA MOTONAO; NOMA MASAKATA |
| PURPOSE: To produce a large amount of human 5-lipoxygenase using microorganism by integrating a gene coding human 5-lipoxygenase into a specific expression vector and expressing in a host. CONSTITUTION: A human 5-lipoxygenase-coding DNA region of E.coli is transformed with an expression vector, the E.coli is proliferated to an extent and the system is added with about 0.2mM of isopropyl-β-D-thiogalactoside to induce the expression of the gene. The medium to be used in the induction is preferably a B medium containing 2% of NaCl and 2% of glycerol and the culture temperature is preferably ≤28°C. The human 5-lipoxygenase accumulated in the cell by the cultivation is recovered and purified by known procedures. The DNA region coding human 5-lipoxygenase is a natural source such as a cDNA library originated from an organ having human 5-lipoxygenase activity. COPYRIGHT: (C)1990,JPO&Japio | ||||||
| 4 | Gene coding human 5-lipoxygenase polypeptide | JP9711488 | 1988-04-20 | JPH02453A | 1990-01-05 | MATSUMOTO TAKASHI; BENKUTO SAMIYUERUSON; KORIN FUANKU; OROFU ROODOMAAKU; YANNOROFU HEEGU; HANSU YANBAARU |
| PURPOSE: To enable the subject polypeptide to be mass-produced by enabling the a gene encoding the above polypeptide to be prepared. CONSTITUTION: A gene (cDNA) coding human 5-lipoxygenase polypeptide having a specific amino acid sequence is prepared. This cDNA can be obtained from a human-derived cDNA library by use of an immunochemical or probe hybridization technique. The cDNA thus obtained can be mass-produced in bacteria as host after inserted into an appropriate vector (e.g. plasmid, phage). The above-mentioned cDNA library has no limitations provided that it is derived from a human organ having 5-lipoxygenase activity. COPYRIGHT: (C)1990,JPO | ||||||
| 5 | A gene coding for human 5-lipoxygenase polypeptide | EP88121407.6 | 1988-12-21 | EP0325773A1 | 1989-08-02 | Matsumoto, Takashi 1-205, Nihontabakosangyo K.K.; Samuelsson, Bengt; Funk, Colin; Radmark, Olof; Höög, Jan-Olov; Jörnvall, Hans |
A synthetic gene which codes for human 5-lipoxygenase. |
||||||
| 6 | Process of producing human 5-lipoxygenase | EP90301898.4 | 1990-02-22 | EP0384750B1 | 1995-11-02 | Matsumoto, Takashi, Life Science Res. Lab.; Noguchi, Masato, Life Science Res. Lab.; Nakamura, Motonao, Life Science Res. Lab.; Noma, Masana Life Science Res. Lab. |
| 7 | Process of producing human 5-lipoxygenase | EP90301898.4 | 1990-02-22 | EP0384750A1 | 1990-08-29 | Matsumoto, Takashi, Life Science Res. Lab.; Noguchi, Masato, Life Science Res. Lab.; Nakamura, Motonao, Life Science Res. Lab.; Noma, Masana Life Science Res. Lab. |
A process of producing human 5-lipoxygenase suited for the mass production of the enzyme is disclosed. In the process of the present invention, E. coli transformed with an expression vector containing a DNA region encoding human 5-lipoxygenase is cultured and the produced human 5-lipoxygenase from the E. coli. is recovered. |
||||||
| 8 | A SOLUBLE AND STABLE HUMAN 5-LIPOXYGENASE | PCT/US2011038492 | 2011-05-31 | WO2011153121A3 | 2012-05-18 | NEWCOMER MARCIA E; BARTLETT SUE G; GILBERT NATHANIEL C |
| A soluble and stable form of 5-lipoxygenase (5-LOX) has been made, 5-Lox is the enzyme which initiates leukotriene biosynthesis by catalyzing the two-step transformation of arachidomc acid to leukotriene A4 (LTA4). The soluble and stable 5-LOX is suitable for a number of applications, including, but not limited to, high throughput screening of 5-LOX inhibitors, structural analysis of the enzyme's active site, designing inhibitors based on the three-dimensional structure of the enzyme's active site, and synthesis of LTA4. Using Stable-5-LOX, the crystal structure for 5-LOX has been resolved and the amino acids defining the active site determined. | ||||||
QQ群二维码
意见反馈
意见反馈