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46 results about "Tricine" patented technology

Tricine is an organic compound that is used in buffer solutions. The name tricine comes from tris and glycine, from which it was derived. It is a white crystalline powder that is moderately soluble in water. It is a zwitterionic amino acid that has a pKa1 value of 2.3 at 25 °C, while its pKa2 at 20 °C is 8.15. Its useful buffering range of pH is 7.4-8.8. Along with bicine, it is one of Good's buffering agents. Good first prepared tricine to buffer chloroplast reactions.

Labeled 99mTc hydrazino-nicotinamide-dioxodecoyl-folic acid coordination compound and preparation method

The invention discloses a labeled 99mTc hydrazino-nicotinamide-dioxodecoyl-folic acid coordination compound with a general formula of 99mTc(HYNIC-NOON-FA)(Tricine)(L). In the structural formula, L is triphenyl sodium phosphate or triphenyl sodium photrisulfonic acid, wherein 1,8-diamido-3,6-octane dioxide is used as a connecting chain for generating a hydrazino-nicotinamide-3,6-dioxodecoyl-folic acid coupler respectively with folic acid and hydrazino-niacin through amido bonds and coordinating with oxygen atoms and phosphorus atoms in a co-ligand Tricine and an L molecule and 99mTc, and the 99mTc(HYNIC-NOON-FA)(Tricine)(L) coordination compound is obtained through two steps of: (a) synthesizing the hydrazino-nicotinamide-3,6-dioxodecoyl-folic acid coupler used as a ligand; and (b) labeling the 99mTc-hydrazino-nicotinamide-dioxodecoyl-folic acid coordination compound. The coordination compound has the advantages of high radiochemical purity, good stability, high tumor intake, good retention, low non-target organ background and clear tumor SPECT (Single Photon Emission Computed Tomography) development and can be prepared into a novel 99mTc labeled folic acid receptor tumor developer widely applied to the technical field of radioactive pharmaceutical chemistry and nuclear medicine.
Owner:BEIJING NORMAL UNIVERSITY +1

Antibacterial lipopeptide of endophytic Bacillus subtilis and separation and purification method

The invention relates to an extracellular antibacterial lipopeptide of plant endophytic Bacillus subtilis Jaasedl and a separation and purification method. The distribution range of the molecular weight of the extracellular antibacterial lipopeptide is mainly between 1,000Da and 2,200Da. The extracellular antibacterial lipopeptide contains an Iturin homologue, a Fengycin homologue and a Surfactin-like Compound homologue. The extracellular antibacterial lipopeptide is a group of uncommon antibacterial lipopeptide mixture produced by a single bacterial strain. The separation and purification method of the extracellular antibacterial lipopeptide comprises the following steps of: after salting out to obtain the crude extract of the antibacterial lipopeptide by using ammonium sulfate from the fermentation liquor of the endophytic Bacillus subtilis Jaasedl, performing Sephedex G-25 molecular sieve chromatography, Cellulose DEAE-52 anion exchange chromatography and FPLC300SB-C18 column chromatography successively, wherein 34 to 37 min of collecting peak has bacteriostatic activity; detecting by Tricine-SDS-PAGE after concentrating; and achieving electrophoretically pure at only one strip to obtain pure extracellular antibacterial lipopeptide. The antibacterial lipopeptide has extremely high research and application value for the development of broad-spectrum antifungal medicaments, and has wide application prospect for natural quality protection of crops and pesticide residue reduction.
Owner:JIANGSU ACAD OF AGRI SCI

Amino acid sequence and polynucleotide sequence for chicken intestinal canal beta alexin and extraction method thereof

A chicken intestinal tract Beta-defensin cDNA is characterized in that the cDNA has the following sequence: tcagacagcc agctgtgcag gaacaaccat ggccactgcc ggaggctctg cttccacatg gagagctggg ctgggagctg catgaacggc cgcctgcgct gctgcaggtt ctccaccaag cagccctttt ccaaccctaa acattcagtg ctgcacacag cagagcagga cccttcccca agccttggag ggacgtga. The amino acid sequence of the Beta-defensin is Ser-Asp-Ser-Gln-Leu Cys-Arg-Asn-Asn-His Gly-His-Cys-Arg- Arg Leu-Cys-Phe-His-Met Glu- Ser-Trp-Ala-Gly Ser-Cys-Met-Asn-Gly Arg-Leu-Arg-Cys-Cys Arg-Phe-Ser-Thr-Lys-Gln Pro-Phe-Ser-Asn-Pro Lys-His-Ser-Val-Leu His-Thr-Ala-Glu-Gln Asp-Pro-Ser-Pro-Ser Leu-Gly-Gly-Thr. The extraction method comprises the following steps of: (1) collecting broken mucosa cells of chicken intestinal tract; (2) breaking vesicles; (3) leaching with 5% acetic acid under stirring, centrifuging, collecting supernatant, removing sediment, subpackaging the supernatant and freeze-storing to obtain crude chicken intestinal tract Beta-defensin; (4) separating the supernatant with Sephadex G-100 gel column at low temperature, eluting with 0.2mol/L sodium acetate (constant flow pump speed 3*1), detecting with nucleic acid-protein detector, collecting the eluate with an automatic collector (1.5mL each tube), and recording with a recorder (speed 6cm/h, and range 20mV); (5) detecting the antibacterial activity of the liquid in each tube to Pasteurella with agarose diffusion method, collecting the eluate with bacteriostatic activity, and storing under vacuum freeze drying; (6) purifying the the eluate with bacteriostatic activity with Tricine-PAGE, PVDF membrane blotting the protein bands, and performing amino acid sequence analysis with Sanger partial hydrolysis method; and (7) deriving chicken intestinal tract Beta-defensin cDNA with BLAST software.
Owner:HENAN AGRICULTURAL UNIVERSITY

Preparation method of anti-aging whey protein peptide

InactiveCN107574214ABest enzymatic hydrolysis processPeptide preparation methodsFermentationDPPHDesorption
The invention discloses a preparation method of anti-aging whey protein peptide, belonging to the technical field of bioactive peptide. The preparation method comprises the following steps: hydrolyzing whey protein concentrate (WPC 80) by adopting alkaline protease, by adopting the degree of hydrolysis and the DPPH free radical scavenging rate as the indexes of evaluation, the hydrolysis and the DPPH free radical scavenging rate as the indexes, adjusting the influences of the following conditions on the hydrolysis effect: the enzyme dosage: 400-10000 U/g, the pH: 8.0, 8.5 and 9.0, the temperatures: 55 DEG C, 60 DEG C and 65 DEG C, the concentration of the substrate: 3-7 %, and the hydrolysis time: 1-6 h, thus the optimal hydrolysis process is obtained, and then enzymolysis is carried out according to the optimal process; hydrolyzing the whey protein concentrate (WPC 80) under the optimal process conditions, desalting the whey protein zymolyte by adopting DA201-C macroporous resin, carrying out dynamic desalting experiment under the following conditions: deionized water and 40-70 % alcohol are adopted as desorption reagents, the sample loading flow rate is 0.5-2.5 mL/min, and the sample loading concentration is 10-50 mg/mL, collecting peptide liquid obtained after desalting, carrying out ultra-filtration separation, and identifying the molecular weight of whey protein peptide byadopting Tricine-SDS-PAGE electrophoresis.
Owner:NORTHEAST AGRICULTURAL UNIVERSITY

Evaluation method of specificity removal effect of haze sensitive protein in yellow wine

InactiveCN104483451AAccurately evaluate the removal effectMaterial analysisDesorptionDecreased protein S
The invention discloses an evaluation method of specificity removal effect of haze sensitive protein in yellow wine, belonging to the field of yellow wine production process. The method comprises the steps of adding a clarifying agent into the yellow wine, collecting protein adsorbed by the clarifying agent, comparing the distribution of molecular weights of haze sensitive protein and protein adsorbed by the clarifying agent by use of the Tricine-SDS-PAGE (Tricine-sodium dodecyl sulfate-polyacrylamide gelelectrophoresis) technology, identifying the types of the haze sensitive protein and the protein adsorbed by the clarifying agent by the MALDI-TOF/TOF MS (Matrix-Assisted Laser Desorption/ Ionization Time of Flight Mass) technology, measuring the total nitrogen content of the yellow wine body before and after the treatment of the clarifying agent by use of a kjeldah method finally, and evaluating that whether the haze sensitive protein is removed and evaluating the removal effect strength according to the identification result that whether the protein adsorbed by the clarifying agent is consistent to the haze sensitive protein by the MALDI-TOF/TOF MS technology and the reduction amount of the protein in the wine body by the kjeldah method. The method can directly and accurately evaluate the removal effect of the clarifying agent on the haze sensitive protein.
Owner:JIANGNAN UNIV
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