Application of cholinesterase in antagonistic tachykinin medicine
What is Al technical title?
Al technical title is built by PatSnap Al team. It summarizes the technical point description of the patent document.
A technology of cholinesterase and tachykinin, which is applied in the application field of medicine to achieve the effects of small side effects, suitable for industrialization, and wide sources
Inactive Publication Date: 2008-06-04
SHENZHEN DINGXIN BIO MEDICINE TECH DEV +2
View PDF3 Cites 3 Cited by
Summary
Abstract
Description
Claims
Application Information
AI Technical Summary
This helps you quickly interpret patents by identifying the three key elements:
Problems solved by technology
Method used
Benefits of technology
Problems solved by technology
There is no report in the literature that cholinesterase is used to prepare drugs for the treatment or prevention of diseases mediated by substance P isotachine
Method used
the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more
Image
Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
Click on the blue label to locate the original text in one second.
Reading with bidirectional positioning of images and text.
Smart Image
Examples
Experimental program
Comparison scheme
Effect test
Embodiment 1
[0070] Embodiment 1 hydrolysis SP test
[0071] Butyrylcholinesterase and acetylcholinesterase, which are used in the market as an enzyme inhibition method to detect pesticide residues, were used to hydrolyze substance P respectively. Reaction and detection conditions:
[0072] 1. Cholinesterase used:
[0073] (1) butyrylcholinesterase, specific activity 200U freeze-dried powder 50mg with 5ml iron ion water (F 3+ Content 1mg / L) dissolved, centrifuged at 10,000 rpm for 4 minutes;
[0074] (2) butyrylcholinesterase, specific activity 200U lyophilized powder 50mg dissolved in 5ml double distilled water, centrifuged at 10000 rpm for 4 minutes;
[0075] (3) Acetylcholinesterase, specific activity 300U freeze-dried powder 20mg dissolved in 1ml double distilled water, centrifuged at 10000 rpm for 4 minutes.
[0076] 2. Substrate
[0077] The purity of SP is 98%, and the concentration of the aqueous solution is 0.5ug / ml.
[0087] Use acetylcholinesterase freeze-dried powder produced by SIGMA company, add water to dissolve, add stabilizer propylene glycol, antibacterial agent phenol at the same time, according to each milliliter solution contains acetylcholinesterase enzyme activity from 10 to 1000U, divide into several orders of magnitude, according to the way of use, pack them separately Disposable syringes, spray bottles, or other medically acceptable vials, kept refrigerated. The storage period can be up to 1 year, and it can be administered directly or diluted according to the treatment requirements.
[0088] Vitality assay:
[0089] 1. Theoretical basis: According to the Ellman method, thioacetylcholine iodide (BTCI) is hydrolyzed into thiocholine and acetic acid under the action of cholinesterase (AChE), and thiocholine can be combined with dithiop-nitrobenzoic acid (DTNB) reacts to generate a yellow product, which has ...
Embodiment 3
[0092] Embodiment 3 aqueous solution 2
[0093] Aqueous solution 1 is added with 5% propylene glycol and 0.5% laurocaprazine as a penetration enhancer, combined with transdermal absorption methods such as iontophoresis or ultrasonic method, for external use.
the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more
PUM
Login to view more
Abstract
The invention belongs to the field of bio-pharmaceutical technology, and discloses the pharmaceutical application of cholinesterase, in particular to the application of cholinesterase in the medicines for treating or preventing the diseases and symptoms mediated by tachykinin in mammals including the human body. The diseases and symptoms include pain, inflammation, central nervous system disease, respiratory disease, gastrointestinal dysfunction and disease, allergy, neuropathological disease, diseases relating to immunopotentiation or immune suppression, rheumatism, skin disease and chronic fatigue syndrome. Being applied in medicines, the cholinesterase provides an effective treatment method with small side effect for people with physiological and pathological changes caused by excessive tachykinin like substance P, etc. The cholinesterase of the invention can be acetylcholinesterase, butyrylcholine esterase, the isoenzyme thereof or the ramification thereof, can derive from the cells, tissues, or blood of animals, or can derive from plants and be obtained through gene recombination. The invention has broad source, does not need to be highly purified, and is suitable for industrialization.
Description
technical field [0001] The present invention relates to a medicine for treating or preventing a disease mediated by a tachykinin, in particular to a cholinesterase which first hydrolyzes an amino acid residue at a C-terminal Leu-Met site to prepare a medicine for treating a disease mediated by a tachykinin in the application. Background technique [0002] Tachykinins (TKs) are a group of peptides with the following series of common amidated carboxy-terminals. Tachykinin C-terminus has -Phe-X-Gly-Leu-Met-NH 2 The common structure is a similar pharmacologically active neuropeptide produced in mammals, including humans, with a variety of physiological functions. The name of tachykinins comes from their stimulating effect on smooth muscle tissue. Mammalian tachykinins mainly include Substance P (Substance P, SP), Neurokinin A (Neurokinin A, NKA) and Neurokinin B (Neurokinin B, NKB). Tachykinins are widely distributed in the central nervous system and peripheral nervous system...
Claims
the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more
Application Information
Patent Timeline
Application Date:The date an application was filed.
Publication Date:The date a patent or application was officially published.
First Publication Date:The earliest publication date of a patent with the same application number.
Issue Date:Publication date of the patent grant document.
PCT Entry Date:The Entry date of PCT National Phase.
Estimated Expiry Date:The statutory expiry date of a patent right according to the Patent Law, and it is the longest term of protection that the patent right can achieve without the termination of the patent right due to other reasons(Term extension factor has been taken into account ).
Invalid Date:Actual expiry date is based on effective date or publication date of legal transaction data of invalid patent.
Login to view more 
Login to view more