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210 results about "Isozyme" patented technology

Isozymes (also known as isoenzymes or more generally as multiple forms of enzymes) are enzymes that differ in amino acid sequence but catalyze the same chemical reaction. These enzymes usually display different kinetic parameters (e.g. different KM values), or different regulatory properties. The existence of isozymes permits the fine-tuning of metabolism to meet the particular needs of a given tissue or developmental stage. In biochemistry, isozymes (or isoenzymes) are isoforms (closely related variants) of enzymes. In many cases, they are coded for by homologous genes that have diverged over time. Although, strictly speaking, allozymes represent enzymes from different alleles of the same gene, and isozymes represent enzymes from different genes that process or catalyse the same reaction, the two words are usually used interchangeably.

Isozyme of autoclavable superoxide dismutase (SOD), a process for the identification and extraction of the SOD in cosmetic, food and pharmaceutical compositions

The invention relates to a novel purified isozyme of an autoclavable superoxide dismutase extracted from the plant Potentilla atrosanguinea Lodd. Var. orgyrophylla, said isozyme having the following characteristics, O2- scavenging activity remains same before and after autoclaving; scavenges O2- from sub-zero temperature of -20° C. to high temperature of +80° C.; O2- scavenging activity at 25° C. for 30 days without adding any stabilizing agent such as polyols or sugars; O2- scavenging activity in the presence of saline (0.9% sodium chloride) to 61.8% of the control (without 0.9% sodium chloride), stable at 4° C. for at least 8 months; contamination free and infection free from any living micro- and/or macro-organism after autoclaving; possesses temperature optima at 0° C.; possesses a molecular weight of 33 kD under non-denaturating conditions; possesses a molecular weight of 36 kD under denaturating conditions; has clear peaks in UV range at 268 and 275 nm; has an enzyme turnover number of 19.53x104% per nmol per min at 0° C.; and requires Cu/Zn as a co-factor, method for the preparation of the purified isozyme of autoclavable superoxide dismutase and formulations containing the said autoclavable superoxide dismutase.
Owner:COUNCIL OF SCI & IND RES

Nicotinamide acids, amides, and their mimetics active as inhibitors of PDE4 isozymes

InactiveUS20020111495A1Organic chemistryDiseasePyridazine
Compounds useful as inhibitors of PDE4 in the treatment of diseases regulated by the activation and degranulation of eosinophils, especially asthma, chronic bronchitis, and chronic obstructuive pulmonary disease, of the formula: wherein j is 0 or 1, k is 0 or 1, m is 0, 1, or 2; n is 1 or 2; A is selected from the partial Formulas: where q is 1, 2, or 3, W3 is -O-; -N(R9)-; or -OC(=O)-; R7 is selected from -H; -(C1-C6) alkyl, -(C2-C6) alkenyl, or -(C2-C6) alkynyl substituted by 0 to 3 substituents R10; -(CH2)u-(C3-C7) cycloalkyl where u is 0, 1 or 2, substituted by 0 to 3 R10; and phenyl or benzyl substituted by 0 to 3 R14; R8 is tetrazol-5-yl; 1,2,4-triazol-3-yl; 1,2,4-triazol-3-on-5-yl; 1,2,3-triazol-5-yl; imidazol-2-yl; imidazol-4-yl; imidazolidin-2-on-4-yl; 1,3,4-oxadiazolyl; 1,3,4-oxadiazol-2-on-5-yl; 1,2,4-oxadiazol-3-yl; 1,2,4-oxadiazol-5-on-3-yl; 1,2,4-oxadiazol-5-yl; 1,2,4-oxadiazol-3-on-5-yl; 1,2,5-thiadiazolyl; 1,3,4-thiadiazolyl; morpholinyl; parathiazinyl; oxazolyl; isoxazolyl; thiazolyl; isothiazolyl; pyrrolyl; pyrazolyl; succinimidyl; glutarimidyl; pyrrolidonyl; 2-piperidonyl; 2-pyridonyl; 4-pyridonyl; pyridazin-3-onyl; pyridyl; pyrimidinyl; pyrazinyl; pyridazinyl; indolyl; indolinyl; isoindolinyl; benzo[b]furanyl; 2,3-dihydrobenzofuranyl; 1,3-dihydroisobenzofuranyl; 2H-1-benzopyranyl; 2-H-chromenyl; chromanyl; benzothienyl; 1H-indazolyl; benzimidazolyl; benzoxazolyl; benzisoxazolyl; benzothiazolyl; benzotriazolyl; benzotriazinyl; phthalazinyl; 1,8-naphthyridinyl; quinolinyl; isoquinolinyl; quinazolinyl; quinoxalinyl; pyrazolo[3,4-d]pyrimidinyl; pyrimido[4,5-d]pyrimidinyl; imidazo[1,2-a]pyridinyl; pyridopyridinyl; pteridinyl; or 1H-purinyl; or A is selected from phosphorous and sulfur acid groups; W is -O-; -S(=O)t-, where t is 0, 1, or 2; or -N(R3)-; Y is =C(R1a)-, or -[N<custom-character file="US20020111495A1-20020815-P00900.TIF" wi="20" he="20" id="custom-character-00001"/>(O)k] where k is 0 or 1; R4, R5 and R6 are (1) -H; provided that R5 and R6 are not both -H at the same time, -F; -Cl; -(C2-C4) alkynyl; -R16; -OR16; -S(=O)pR16; -C(=O)R16, -C(=O)OR16, -C(=O)OR<highlight><sup
Owner:PFIZER INC

Novel isozyme of autoclavable superoxide dismutase (SOD), a process for the identification and extraction of the SOD and use of the said SOD in cosmetic, food, and pharmaceutical compositions

The invention relates to a novel purified isozyme of an autoclavable superoxide dismutase extracted from the plant Potentilla astrisanguinea Lodd. Var. orgyrophylla, said isozyme having the following characteristics, O2-. scavenging activity remains same before and after autoclaving; scavenges O2-. from sub-zero temperature of -20° C. to high temperature of +80° C.; O2-. scavenging activity at 25° C. for 30 days without adding any stabilizing agent such as polyols or sugars; O2-. scavenging activity in the presence of saline (0.9% sodium chloride) to 61.8% of the control (without 0.9% sodium chloride), stable at 4° C. for at least 8 months; contamination free and infection free from any living micro- and / or macro-organism after autoclaving; possesses temperature optima at 0° C.; possesses a molecular weight of 33 kD under non-denaturating conditions; possesses a molecular weight of 36 kD under denaturating conditions; has clear peaks in UV range at 268 and 275 nm; has an enzyme turnover number of 19.53x104% per nmol per min at 0° C.; and requires Cu / Zn as a co-factor, method for the preparation of the purified isozyme of autoclavable superoxide dismutase and formulations containing the said autoclavable superoxide dismutase.
Owner:COUNCIL OF SCI & IND RES

Protein kinase c epsilon as modulator of anxiety, alcohol consumption and self-administration of drugs of abuse

The present invention is directed to the production of PKC isozyme epsi (PKCepsi)-deficient cells and non-human animals. The present invention is further directed to the identification of PKCepsi as a target for drugs that reduce anxiety. According to the present invention, PKCepsi-inhibiting compounds act in synergy with drugs acting at the GABAA receptor. The present invention is also directed to the use of modulators of PKCepsi to modulate alcohol consumption, self-administration of other drugs of abuse, and the effects of alcohol consumption as well as the use of inhibitors of PKCepsi, either alone or in conjunction with allosteric agonists of GABAA receptors, to treat conditions, such as addiction, withdrawal syndrome, skeletal muscle spasms, convulsive seizures, and epilepsy, that are amenable to treatment by allosteric agonists of GABAA receptors. Additional aspects of the present invention are diagnostic methods for identifying individuals at risk for becoming alcoholics or abusers of other drugs and kits for performing such diagnostic methods. The present invention relates to: cells and non-human animals deficient for the PKC isozyme epsi (PKCepsi); the use of PKCepsi as a target for drugs; the use of inhibitors of PKCepsi in methods of reducing anxiety and treating conditions associated with insufficient activity of the GABAA receptor; the use of modulators of PKCepsi in methods of modulating alcohol consumption, modulating self-administration of other drugs of abuse, and altering the effects of alcohol; pharmaceutical compositions comprising inhibitors of PKCepsi and allosteric agonists of GABAA receptors; and the identification of individuals with enhanced susceptibility to alcoholism or other forms of addiction.
Owner:GALLO CLINIC & RES CENT +1

Method for degrading octyl phenol by utilizing laccase

The invention discloses a method for degrading octyl phenol by utilizing laccase. The method comprises the steps of: preparing a LacA enzyme solution; adjusting the concentration of the octyl phenol within 25-200 mg / L; adding the laccase having a concentration of 0.5-3 U / mL in the LacA enzyme solution; controlling the pH of a reaction system to 3.5-6; and degrading under the condition of keeping the temperature at 25-50 DEG C. As a bio-enzyme catalysis technology is adopted, the method for degrading the octyl phenol by utilizing the accase has outstanding characteristics of high removal efficiency, good convenience and safety, no pollution and the like. By comparing specifity of different isozymes to the octyl phenol, selecting the laccase having the strongest specifity to the octyl phenol and adding a medium substance, the method for degrading thhe octyl phenol by utilizing the laccase increases the reaction efficiency of the laccas, redudes reaction time, therefore reduces usage amount of the laccase, and lowers operating cost. The method for degrading the octyl phenol by utilizing the laccase can degrade octyl phenol efficiently and can obtain the degradation rate up to 97.2% after 12-hour reaction under a suitable catalysis condition when the concentration of the octyl phenol is 100 mg / L.
Owner:NANJING FORESTRY UNIV

Therapeutic and diagnostic methods dependent on cyp2a enzymes

InactiveUS20070254921A1BiocideNervous disorderCytochromeTobacco Dependences
A method of regulating the activity of human cytochrome P450 isozyme CYP2A6 to control nicotine metabolism or decrease to production of carcinogens from procarcinogens, such as those present in tobacco smoke, in an individual by selectively inhibiting CYP2A6. Various prophylactic (i.e., prevention and treatment) compositions and methods are also described, including an improved oral nicotine composition and method comprising the use of nicotine together with an inhibitor of the CYP2A6 enzyme. Furthermore, it has been discovered that the presence in an individual of a mutant allele of human cytochrome P450 enzyme CYP2A6 (referred to throughout this specification as “CYP2A6” for brevity) is predictive of an individual who: (i) has a decreased risk of becoming a smoker, (ii) will smoke less if he / she becomes dependent, and / or (iii) may be at relatively lower risk for cancer due to both decreased smoke exposure and decreased CYP2A6-mediated activation of tobacco smoke and other procarcinogenic substrates. This invention provides diagnostic methods for predicting tobacco dependence risk and risk for cancers related to CYP2A6 substrates in an individual by analysing for the presence of a mutant genotype for human cytochrome P450 enzyme CYP2A6 in an individual, ranging from gene duplication (multiple copies of CYP2A6) to single or even no copies due to null alleles or gene deletion.
Owner:NICOGEN

Tea polyphenol oxidase isozyme monomers PP01 and PP02 and preparation method thereof

The invention discloses tea polyphenol oxidase isozyme monomers PP01 and PP02 and a preparation method thereof. With respect to the technical states that existing tea polyphenol oxidase is low in purification factor, low in loading quantity of protein samples and long in operation time, the obtained isozyme is the isozyme with one relative molecular weight, and the isozyme monomer with specific amino acid sequence structure, molecular weight, isoelectric point, enzymatic property and the like cannot be obtained, two tea polyphenol oxidase isozyme monomers with specific specific amino acid sequence structures, molecular weight, isoelectric points, enzymatic properties and the like are separated and prepared by sequentially adopting the technologies and optimization processes such as enrichment of zymoprotein with acetone powder, fractional precipitation of ammonium sulfate, strong anion exchange chromatography, gel medium chromatography, molecular identification and enzymatic property analysis. The method has the advantages of low cost, large preparation amount, high pertinence, short operation cycle and the like, and is of important theoretical and practical significance on deepening of the separation and purification technology of tea polyphenol oxidase isozyme, promoting of directional enzymatic synthesis of a theaflavin component by virtue of the tea polyphenol oxidase isozyme monomers, development and utilization of advantaged isozyme of tea polyphenol oxidase, isozyme immobilization, enzyme protein structure analysis, enzyme gene cloning, functional verification and the like.
Owner:HUNAN AGRICULTURAL UNIV
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