35 results about "Phenylalanine+Tyrosine" patented technology

A method of cell culture comprising providing cells in a cell culture medium to start a cell culture process, and, maintaining at least one metabolite selected from 3-(4-hydroxyphenyl)lactate, 4-hydroxyphenylpyruvate, phenyllactate, indolelactate, indolecarboxylic acid, homocysteine, 2-hydroxybutyric acid, isovalerate and formate below a concentration C1 in the cell culture medium, wherein C1 is 3 mM and / or (ii) maintaining at least one amino acid selected from phenylalanine, tyrosine, tryptophan, methionine, leucine, serine, threonine and glycine below a concentration C2 in the cell culture medium, wherein C2 is 2 mM.

A method of cell culture comprising providing cells in a cell culture medium to start a cell culture process, and,maintaining at least one metabolite selected from 3-(4-hydroxyphenyl)lactate, 4-hydroxyphenylpyruvate, phenyllactate, indolelactate, indolecarboxylic acid, homocysteine, 2-hydroxybutyric acid, isovalerate and formate below a concentration C1 in the cell culture medium, wherein C1 is 3 mM and / or(ii) maintaining at least one amino acid selected from phenylalanine, tyrosine, tryptophan, methionine, leucine, serine, threonine and glycine below a concentration C2 in the cell culture medium, wherein C2 is 2 mM.

The invention relates to a combined ligand, a combined bionic chromatography medium and a preparation method and application thereof. The combined bionic chromatography medium uses hydrophilic porousmicrospheres as chromatography matrix, is activated by allyl bromide, is brominated and alcoholized by N-bromosuccinimide, and then is coupled with the combined ligand. The sequence of the combined ligand is phenylalanine-tyrosine-glutamic acid-5-aminobenzimidazole. The combined bionic chromatography medium has two functional groups including phenylalanine-tyrosine-glutamic acid tripeptide and aminobenzimidazole, introduces a hydrophobicity charge-inducing ligand while retaining the high selectivity characteristic of a polypeptide ligand to an antibody, makes elution conditions milder, and achieves effective antibody isolation.

This invention relates to a hybrid ligand, a hybrid biomimetic chromedia and a preparing method and a use thereof, wherein the hybrid biomimetic chromedia takes hydrophilic porous microsphere as a substrate in chromatography, activated with allyl bromide and undergoing bromo-alcoholization with N-bromosuccinimide, then coupled with the hybrid ligands. The sequence of the hybrid ligand is phenylalanine-tyrosine-glutamine-5-aminobenzimidazole. The hybrid biomimetic chromedia has both of the two functional groups of phenylalanine-tyrosine-glutamine tripeptide and aminobenzimidazole, while maintaining the high antibody selectivity of polypeptide ligand, hydrophobic electric charge inductive ligand is introduced to achieve more moderate elution requirement, realizing effective antibody separation.

The invention relates to a method for separating immune globulin IgG from human serum. The method comprises the following steps: 1) diluting the human serum by a buffer solution, adjusting a pH to 6.0to 8.0 and filtering by a filter membrane to obtain a human serum sample; 2) feeding the human serum sample into a chromatographic column, washing by a balancing buffer solution, then eluting by a eluting buffer solution and collecting eluent to obtain the immune globulin IgG solution, the chromatographic column is filled with a combined type bionic chromatography medium, the combined type bionicchromatography medium is prepared from a chromatography matrix and combined type ligand, the chromatography matrix is a hydrophilic porous microsphere with hydroxyl, and a sequence of the combined type ligand is phenylalanine-tyrosine-glutamine-5-aminobenzimidazole; 3) performing utlrafiltration and concentration on the immune globulin IgG solution to obtain the immune globulin IgG. The method can improve an efficiency and a purity for separating the immune globulin IgG from blood.

The invention discloses a method and equipment for separating and extracting amino acid products from protein hydrolyzate, comprising the following steps: diluting the amino acid mixed solution with water, making it flow through a type I column, washing with water, and then flowing the amino acid mixed solution with ethanol hydrochloric acid After passing through the chromatographic column, combine the washing liquid and the mixed solution of ethanol hydrochloric acid and adjust the collected liquid to a pH value of 5.0~6.0, filter to obtain tyrosine, then neutralize the filtrate with alkali until the pH value is greater than 7.0, and pass it through Type III column to separate phenylalanine, tyrosine and / or tryptophan; adjust the pH value of the mixed solution of amino acids flowing through the type I column to be greater than 7.0, make it flow through the type II column, and then adopt Washing with water, freeing with hydrochloric acid, collecting the washing liquid in sections to obtain the separation solution of bright component, preserved component and C component; and then performing subsequent separation on these separation solutions to obtain all amino acid products. This method can increase the number of single amino acid varieties and yield The water body in the separation and extraction can be recycled, and the waste water meets the environmental protection discharge requirements.

The invention discloses a method for preparing quinoline compounds by catalyzing zirconocene dichloride. The method uses 3-butyne-2-ketone compounds and anthranilobenzenethiol compounds as raw materials, As a catalyst, L-phenylalanine, tyrosine, etc. are used as catalyst ligands, N,N-dimethylformamide is used as a solvent, and elemental iodine, hydrogen peroxide, tert-butanol peroxide, etc. are used as oxidants, The quinoline compounds can be prepared efficiently and in high yield. The catalyst used in the present invention is low in cost, stable to air, mild in reaction conditions, and simple in operation. After the reaction is completed, the product is extracted and washed and separated by simple column chromatography to obtain quinoline compounds, which are quinoline compounds The preparation of opens a low-cost and high-efficiency way, and has broad application prospects.

The invention relates to the technical field of amino acid preparation, in particular to a spider silk hydrolyzate and a preparation method thereof. The spider silk hydrolyzate is prepared by the following steps: crush the spider silk, mix the crushed spider silk with sodium hydroxide solution, hydrolyze at 80-90°C for 4-5 hours, and centrifuge to obtain a hydrolyzate; adjust the hydrolyzate The pH value is 4.0-5.5, and the 200nm membrane is filtered to obtain the spider silk hydrolyzate. The amino acid hydrolysis yield of the preparation process of the present invention is 74.15%-80.89%, and the yield is >70%; in the hydrolyzate, methionine is not detected, except for phenylalanine and tyrosine, the yields of other amino acids are all >60% . That is, the distribution of amino acids in the hydrolyzate is basically consistent with that in spider silk. In the hydrolyzate, small molecule peptides with a molecular weight of 1000‑5000D accounted for 72.18% to 76.69%, indicating that the spider silk hydrolyzate not only maintains the original beauty and medical effects of moisturizing, repairing, firming and anti-wrinkle, but also is easily destroyed Human body absorbs.

The invention discloses an affinity biomimetic chromatography medium with a tetrapeptide as a functional ligand, wherein the affinity biomimetic chromatography medium can be used for antibody separation and purification, and the amino acid sequence of the tetrapeptide is phenylalanine-tyrosine-tryptophan-arginine. The preparation method comprises: activating with allyl bromide, carrying out bromination alcoholization, linking a space arm hexanediamine to a polysaccharide gel, and conjugating with an acetylated phenylalanine-tyrosine-tryptophan-arginine tetrapeptide ligand to obtain the tetrapeptide chromatography medium. According to the present invention, the tetrapeptide chromatography medium has good adsorption capacity to antibodies, has high selectivity, can adsorb antibodies under weak alkaline (pH value of 8.0) conditions, can be eluted under weak acidic (pH value of 5.0) conditions, has mild separation conditions, and can be used for isolating immunoglobulins from human serum and isolating monoclonal antibodies in cell culture.

The invention discloses Hericium erinaceus mycelium and a cultivation method thereof. It contains relatively high content of amino acids and vitamins, and also contains 7 kinds of cyclic dipeptides, ergosterol and carboxymethyl cellulase activity. The 7 kinds of cyclic dipeptides are respectively For: cyclic (valine-tyrosine), cyclic (leucine-tyrosine), cyclic (phenylalanine-tyrosine), cyclic (phenylalanine-phenylalanine), cyclic (leucine‑leucine), ring (leucine‑alanine), ring (valine‑alanine). The cultivation method includes mother strain cultivation, original strain cultivation, cultivar strain cultivation, a "directed" biotransformation process and a secondary "directed" biotransformation process. The cultivated Hericium erinaceus mycelium has good anti-tumor effect.