37 results about "Dimethyl-L-arginine" patented technology

The invention relates to a latex enhanced immunoturbidimetry kit for the detection of asymmetric dimethylarginine content. Specifically, the invention relates to a latex enhanced immunoturbidimetry kit for the detection of asymmetric dimethylarginine (ADMA) content in human blood samples. The kit comprises a mouse anti-human monoclonal antibody solution, an ADMA-human Serum albumin complex crosslinked latex particle expansion and an ADMA calibrator. According to the method, by the utilization of competitive binding of free ADMA in blood and ADMA crosslinked on the surface of latex particles to ADMA monoclonal antibody, turbidity formed by the reaction between the ADMA-crosslinked latex particles and ADMA monoclonal antibody is reduced. Therefore, the content of ADMA is detected through the reduction degree of turbidity. The kit provided by the invention can be applied in a biochemical analyzer commonly-used in clinic, is convenient and rapid to operate and has strong specificity. Both sensitivity and detection range of the kit can satisfy clinic application needs.

The present invention relates to novel arginine analogs, and methods for their synthesis and use. Such analogs are designed to provide a protected or free thiol (—SH) group, thereby providing a convenient linkage chemistry for coupling to a suitable group on a target such as a protein, polypeptide, detectable label or solid phase, and at a site distal to the guanidino group. Arginine analog conjugates are useful for generating antibodies that can bind specifically with dimethylarginine, which can be detected using such antibodies in immunoassays.

Method of detecting Symmetrical dimethyl arginine (SDMA) in biological samples. SDMA analogs for generating anti-SDMA antibodies having little or no cross-reactivity with asymmetrical dimethyl arginine, arginine, and monomethylarginine. The analogs have a protected or free thiol (—SH) group or hydroxyl (—OH) group that allow them to be linked to a suitable conjugation target which can be, for example, a protein containing molecule of a label. The anti-SDMA antibodies can be used in diagnostic immunoassay for the diagnosis of SDMA associated disorders and/or diseases.

The present invention provides methods of detecting asymmetric dimethylarginine (ADMA) in a sample, particularly a sample that may contain symmetrical dimethylarginine (SDMA) and/or arginine. The methods generally involve modifying any SDMA and arginine in the sample such that SDMA and arginine are readily distinguishable from ADMA; and detecting ADMA. The invention further provides antibodies specific for ADMA; antibodies specific for modified SDMA; and antibodies specific for modified arginine. The invention further provides kits for practicing the subject methods.

The invention relates to a method for measuring the concentration of asymmetric dimethylarginine and a diagnostic reagent kit. The method comprises the following steps of: degrading asymmetric dimethylarginine (ADMA) by adopting dimethylarginine dimethylamino hydrolase to generate dimethylamine and citrulline; reacting the citrulline with adenosine triphosphate (ATP) and aspartate under the action of arginine succinate synthetase to generate adenosine monophosphate (AMP); generating inosine monophosphate (IMP) and ammonia by the AMP under the action of AMP deaminase; generating oxidization nicotinamide adenine dinucleotide (NAD) by the ammonia and deamination NAD under the action of NAD synzyme; and calculating the concentration of the ADMA by detecting the concentration of the NAD. The method and the reagent kit are accurate in results, and high in speed, repeatability and interference resistance, and are convenient to popularize and use.

The invention discloses a measuring method of asymmetric dimethylarginine concentration, comprising the steps of: subjecting a sample to be measured to a reaction in an enzymatic cycling reaction system, measuring and calculating the generation rate of ammonia from the enzymatic cycling reaction, thus obtaining the content of asymmetric dimethylarginine in the sample to be measured. The enzymatic cycling reaction system consists of dimethylarginine dimethylaminohydrolase, citrullinase, ornithine carbamoyltransferase, and carbamyl phosphate or its salt. The invention also discloses a measuring reagent corresponding to the method. In the invention, an enzymology measuring method and a measuring reagent of asymmetric dimethylarginine are established for the first time. Needing no special instrument, the method of the invention has simple operation, high sensitivity and low cost, thus being able to realize rapid and high flow sample detection in clinic. Thus, asymmetric dimethylarginine is probable to become a conventional inspection item in clinic. Therefore, the method provided in the invention is of great scientific and economic value.

The invention discloses a reagent kit and method for measuring the concentration of asymmetric dimethylarginine. The reagent kit comprises a reagent 1 and a reagent 2, wherein the reagent 1 is prepared from latex particles coated with monoclonal antibodies resisting asymmetric dimethylarginine, and the reagent 2 is prepared from latex particles coated with asymmetric dimethylarginine-inert carrier conjugates. When the reagent kit is adopted for detecting asymmetric dimethylarginine, immune turbidity can be easily improved, detection signals can be easily amplified, the reagent kit has the advantages of being free of special instruments, easy and convenient to operate, high in sensitivity and low in cost, rapid and large-flow clinical sample testing can be achieved, it is made possible that asymmetric dimethylarginine becomes a clinical conventional detection item, and the reagent kit has high economic value.

The invention relates to a urine protein marker for ovarian cancer and abdominal cavity transplantation tumors and diagnosis application thereof, in particular to a urine protein marker obtained by using a rat ovarian cancer cell abdominal cavity transplantation tumor model and mass spectrometry, and application in diagnosis and disease course monitoring of human ovarian cancer and abdominal cavity transplantation tumors. The urine protein marker is selected from cell adhesion molecules 4, alcohol dehydrogenase 1, N(G), N(G)-dimethylarginine 1, methyl mercaptan oxidase, phosphotriesterase related protein, an Rab GDP dissociation inhibitor beta and the like. Urine differential protein obtained from the marker provides simpler, quicker and non-invasive choice for early diagnosis and diseasecourse monitoring of ovarian cancer and abdominal cavity transplantation tumors.

The present disclosure provides DDAH modulators. Thus, the present disclosure provides a method of treating a patient suffering from a disorder characterized by excessive NO production and/or elevated DDAH activity, the method comprising administering to said patient an effective amount of a compound of one of formulae I-X. The present disclosure also provides a pharmaceutical composition comprising a compound of one of formulae I-X.

The invention relates to a biological enzyme method for measuring NG, NG<'>dimethyl-L-arginine or asymmetric dimethylarginine (ADMA) and kit development. Particularly, the biological enzyme method and a kit are characterized in that under the effect of dime-thylarginine dimethyl amino hydrolase (DDAH), the ADMA generates dimethylamine and L-citrulline which are equal in amount, and the L-citrulline is converted into L-ornithine, ammonia and carbon dioxide which are equal in amount through omithine transcarbamoylase, EC2.1.3.3 and carbamatekinase, EC2.7.2.2. The content of the ammonia is measured with a diacetyl monoxime-thiosemicarbazide colorimetric method or a glutamate dehydrogenase rate method, and then the concentration of the ADMA in serum is inferred. The biological enzyme method and the kit have the advantages that reaction steps and reaction conditions are simplified, good repeatability, good accuracy, good sensitivity and good stability are achieved, the rapid requirement, the mass requirement and the economical requirement of clinical detection are met, and application and popularization are facilitated.

The invention relates to the technical field of measuring and testing and discloses an enzymological detection method for detecting concentrations of citrulline, asymmetric dimethylarginine and the like in a reaction system by ATP (adenosine triphosphate) detection. According to the basic principle of reaction, ADMA (asymmetric dimethylarginine) is hydrolyzed by dimethylarginine dimethylaminohydrolase to obtain citrulline; in the presence of ADP (adenosine diphosphate) and Mg2+, the citrulline is subjected to coupling catalysis through ornithine carbamoyl transferase and carbamyl phosphokinase to finally obtain ornithine, carbon dioxide, ammonia, and ATP, and the released ATP is detectable by reagents. The enzymological detection method has the main advantages that reaction is sensitive, quick and highly accurate, the price is low, the ADMA or citrulline with the least concentration of 0.1 micromol/L can be detected, the detected concentration is approximate to the concentration of the ADMA in normal physiological serum and is far lower than the concentration of citrulline in the normal physiological serum, and a new available method for clinical ADMA detection is provided.

The invention discloses an asymmetric dimethylarginine high-efficiency detection method. The method is suitable for detecting content of asymmetric dimethylarginine in a sample, and the method comprises the following steps: obtaining an asymmetric dimethylarginine quantitative criterion rectification curve; preparing a detection product; separating the asymmetric dimethylarginine by high-flux liquid chromatography; detecting the asymmetric dimethylarginine by tandem mass spectrometry; and obtaining the content of the asymmetric dimethylarginine. The method uses the high-flux liquid chromatography-tandem mass spectrometry for rapidly and efficiently detecting the content of the asymmetric dimethylarginine in a biological sample.

The invention belongs to the technical field of medical biology, and particularly discloses a marker and a kit for diagnosing esophageal squamous carcinoma. The marker for diagnosing the esophageal squamous carcinoma, provided by the invention, is at least one of S-sulfo-L cysteine, symmetric dimethylarginine and 4-methoxyphenylacetic acid, and a detection reagent of the marker can be used for preparing a product for diagnosing the esophageal squamous carcinoma. The invention also provides a kit for diagnosing esophageal squamous carcinoma, the kit contains a detection reagent for detecting the marker, and the detection reagent is a reagent for detecting the marker in a sample through chromatography-mass spectrometry or chromatography-mass spectrometry. By detecting the expression levels of S-sulfo-L cysteine, symmetric dimethylarginine and 4-methoxyphenylacetic acid in human serum, esophageal squamous cell carcinoma can be effectively detected, the detection sensitivity reaches up to 80%, the specificity reaches up to 71%, and the kit can be used for large-scale screening of asymptomatic crowds in high-incidence areas of esophageal squamous cell carcinoma, and screening and early detection of asymptomatic high-risk groups are facilitated.

The invention relates to a mutant protein comprising at least a fragment of a mutant dimethylarginine dimethylaminohydrolase (DDAH) enzyme, wherein the fragment possesses an affinity for asymmetric N,N-dimethyl arginine (ADMA) and/or L,N-monomethylarginine (LNMMA), which exists at lower plasma levels than ADMA, and is deficient in hydrolyzing ADMA or LNMMA to citrulline, releasing citrulline, or both.

The present invention belongs to the technical field of immunotherapy. A method of using dimethylarginine derivatives to inhibit the proliferation of lymphocyte. ADMA, SDMA, and their derivative DMGV can inhibit T cells and/or B cells proliferation in vitro by inducing mitochondrial ROS. ADMA and SDMA can induce mitochondrial ROS generation by the action of alanine-glyoxylate aminotransferase 2 (AGXT2), which converts both ADMA and SDMA into dimethylguanidino valeric acid (DMGV) in the mitochondria. The dimethylarginine dimethylamino hydrolase (DDAH) inhibitor PD404182 also inhibits T cell proliferation by allowing more ADMA and SDMA to be converted to DMGV. As a clinical relevance, DMGV effectively treated arthritis in mice which was caused by activated T cells.