61 results about "Lysine arginine" patented technology

The invention is methods and related kits for diagnosing a disease state of cachexia by measuring biomarker profiles from a biological sample. Rapid measurement of early onset or progression of the disease in a subject is determined by measuring biomarker levels from the subject and optionally comparing the biomarker levels to a standard biomarker profile or metabolome phase portrait for the disease. The biomarkers measured in the assay and related kit for cachexia progression include biomarkers selected from the group consisting of lactate, citrate, formate, acetoacetate, 3-hydroxy butrate, alanine, glutamine, glutamate, valine, isoleucine leucine, thrionine, lysine, arginine, tyrosine, phenyl alanine, histidine and tryptophan.

The invention discloses a method for preparing coffee reaction flavor through Maillard reaction. The method is characterized by comprising the following steps: taking baked coffee powder, reducing sugar and complex amino acids as raw materials and water and propylene glycol as solvents to carry out Maillard reaction under heating condition to prepare the coffee reaction flavor, wherein the complex amino acids are at least four of lysine, arginine, glutamic acid, histidine, glycine and leucine. The method has the following beneficial effects: the gaps in preparation and application of the coffee reaction flavor at home and abroad are filled in and the problem of too high cost caused by only adding coffee extracts to the food and cigarettes is effectively solved at the same time.

The invention relates to hyperbranched polyamino acid. The chemical composition is as follows: in the formula of (Lys-)a-(-Arg-)b-(-His-)c-(-X)d, Lys, Arg and His are respectively lysine, arginine and histidine, X is one of or a plurality of any amino acids except for the amino acids above, wherein a is not less than 0.2 and not more than 0.95, b is not less than 0 and not more than 0.8, c is not less than 0 and not more than 0.8, d is not less than 0 and not more than 0.3, and the sum of a, b, c and d is 1. The preparation method is as follows: uniformly mixing lysine or lysine salt with other amino acids or the amino acid salts contained in the hyperbranched polyamino acid to react for 2-64h at the temperature of 130-180 DEG C and then obtain yellow solid, and finally purifying the coarse product with a precipitation method to obtain the hyperbranched polyamino acid. The hyperbranched polyamino acid obtained in the invention can be used as nonviral gene carrier for the transduction of huamn or animal cell gene, and the hyperbranched polyamino acid nonviral gene carrier provided by the invention is reasonable in design, simple in preparation method, high in transfection efficiency, low cytotoxicity and favorable transduction efficiency in the presence of blood serum.

An antibacterial peptide LZ1 is an artificially designed and synthesized active polypeptide and contains 15 amino acid residues, the molecular weight is 2,228.77Da, and the isoelectric point is 12.05; and the full sequence of the antibacterial peptide is valine-lysine-arginine-tryptophan-lysine-lysine-tryptophan-tryptophan-arginine-lysine-tryptophan-lysine-lysine-tryptophan-valine-NH2. The antibacterial peptide LZ1 is small in molecular weight, strong in bactericidal effect and wide in antibacterial spectrum, almost does not have hemolytic activity or eukaryocyte toxicity, is a small molecular antibacterial peptide with application value, is convenient to artificially synthesize, and can be used for preparing an antibacterial medicament.

The invention relates to a variant cathelicidin-BF15 of bungarus fasciatus antibiosis peptide cathelicidin-BF and application thereof. The invention belongs to the field of biomedicine. The variant cathelicidin-BF15 of the bungarus fasciatus antibiosis peptide cathelicidin-BF is a straight chain polypeptide which contains 15 amino acid residues with the molecular weight of 1,939.47Da and an isoelectric point of 12.05. The total sequence of the cathelicidin-BF15 is as follows:valine-lysine-arginine-phenylalanine-lysine-lysine-phenylalanine-phenylalanine-arginine-lysine-leucine-lysine-lysine-serine-valine. The cathelicidin-BF15 which has strong bactericidal action can exterminate a plurality of clinical drug-fast bacteria. In addition, the cathelicidin-BF15 is also characterized by simple structure, convenient synthesis, broad spectrum antibiosis, and the like.

A composition of a long-acting enzyme comprises the enzyme in a formulation comprising a buffer and an additive selected from the group consisting of tranexamic acid, ε-aminocaproic acid, and analogs of L-lysine other than tranexamic acid and ε-aminocaproic acid, combinations thereof, and mixtures thereof. The composition can further comprise another additive selected from the group consisting of L-lysine, L-arginine, L-ornithine (or its pharmaceutically acceptable salts; e.g., L-ornithine hydrochloride), γ-aminobutyric acid, 5-aminovaleric acid, 7-aminoheptanoic acid, glycylglycine, triglycine, N-α-acetyl-L-arginine, betaine, sarcosine, gelatin, HSA, streptokinase, tPA, uPA, non-ionic surfactants, glycerin, D-sorbitol, combinations thereof, and mixtures thereof. A method for prolonging the activity of an autodegradable enzyme comprises storing the enzyme after manufacture at a low pH, and reconstituting the acidified enzyme before use with a solution containing at least one of such additives. The method is useful to provide enzyme for wide use, which otherwise would lose activity upon long storage. In one embodiment the method is applicable to provide enzyme for inducing controlled posterior vitreous detachment.

The invention belongs to the technical field of a premix feed for laying hens and in particular discloses a premix feed for increasing egg yield during the laying hen egg-producing period. The feed consists of the following raw materials in part by weight: 50-500mg of vitamin A, 500-2000mg of vitamin B1, 500-2000mg of vitamin B2, 1000-5000mg of vitamin C, 10-50mg of vitamin D3, 1000-5000mg of vitamin E, 200-1000mg of vitamin K3, 500-1500mg of vitamin PP, 200-1000mg of folic acid, 1000-5000mg of methionine, 1000-5000mg of lysine, 1000-5000mg of arginine, 1000-5000mg of vingine, 5-20g of astragalus polysaccharide, and 50-150mg of an antioxidant, and the auxiliary materials are added until the total amount is 1kg. The premix feed is rich in nutrition and reasonable in matching, and the laying hen can be promoted to lay more eggs.

The invention relates to an antimicrobial peptide Pc-CATH1 from Phasianus colchicus and a gene thereof, a chemical synthesis method and application in the field of biopharmaceuticals and belongs to the technical field of biomedicine. The antimicrobial peptide Pc-CATH1 is a straight-chain polypeptide encoded by (Phasianus colchicus) Cathelicidin genes, and the complete sequence of the antimicrobial peptide Pc-CATH1 is as follows: arginine-isoleucine-lysine-arginine-phenylalanine-tryptophan-proline-valine-valine-isoleucine-arginine-threonine-valine-valine-alanine-glycine-tyrosine-asparaginate-leucine-tyrosine-arginine-alanine-isoleucine-lysine-lysine-lysine; and a gene for encoding a precursor of the antimicrobial peptide Pc-CATH1 consists of 607 nucleotides, wherein the 367th to 445th nucleotides are used for coding mature peptide part. The antimicrobial peptide Pc-CATH1 is smaller in molecular weight, stronger in bactericidal action and broader in spectrum and has strong effect of killing various clinical drug-resistant bacteria; the antimicrobial peptide Pc-CATH1 has a simple structure without a disulfide bond or a ring structure and is convenient for chemical synthesis and the preparation of gene engineering; and in addition, the antimicrobial peptide Pc-CATH1 has the beneficial characteristics of no hemolysis, no cytotoxicity, super-strong serum stability and the like.

The invention provides a deodorizing and purifying concentrated solution, and a preparation method and an application thereof. The deodorizing and purifying concentrated solution comprises lysine, arginine, glycine, taurine, trehalose, an antibacterial saccharide compound, glycerol monoalkyl ester, a bactericide, a solubilizer and water. The deodorizing and purifying concentrated solution providedby the invention has the following advantages: through mutual cooperation of all components, the synergistic effect is achieved; peculiar smell molecules in the environment can be rapidly captured; organic matter generating odor can be decomposed or neutralized; the source of generated odor gas is reduced; the generated odor gas can be eliminated in time; various common bacteria or fungi can be restrained; the action time is short; the inhibition effect is strong; meanwhile, the deodorizing and purifying concentrated solution can be directly sprayed or diluted and then sprayed onto the body or hair of a pet, and is safe, reliable and low in irritation.

This invention relates to a method of immobilizing biocatalysts including protein and cells by co-precipitation with silicate or organosilicate matrices through the action of an organic template molecule. The organic template molecule is in general a polyamine such as polyethylenimine (PEI), or polypeptide compound bearing at least two or three basic residues selected from the group consisting of lysine, arginine, histidine, proline, hydroxyproline, N-methylhistidine, ornithine, taurine, δ-hydroxylysine, and δ-hydroxy-ω-N,N,N trimethyllysine. The invention is also directed to a silica biocomposite comprising co-precipitates of active biocatalysts, silica or organosilicates, and an N-containing organic template molecule. Such silica biocomposites are useful in biocatalysis, and other applications requiring an immobilized biocatalyst. Preferred biocatalysts for this invention are enzymes and whole cells.

The present invention addresses the problem of generalizing and improving a DNA-binding protein in which a PPR is used. Provided is a protein including at least one PPR motif having a structure represented by formula (1), wherein one PPR motif (Mn) included in the protein is a PPR motif having three amino acids of No. 1 A.A., No. 4 A.A., and No. ''ii'' (-2) A.A., in a combination of specific aminoacids corresponding to a target DNA base or a target DNA base sequence, and satisfies at least one selected from the group consisting of the following (a)-(h): (a) No. 7 A.A. in the PPR motif (Mn) isisoleucine (I); (b) No. 9 A.A. in the PPR motif (Mn) is alanine (A); (c) No. 10 A.A. in the PPR motif (Mn) is tyrosine (Y); (d) No. 18 A.A. in the PPR motif (Mn) is lysine (K), arginine (R), or histidine (H); (e) No. 20 A.A. in the PPR motif (Mn) is glutamic acid (E) or aspartic acid (D); (f) No. 29 A.A. in the PPR motif (Mn) is glutamic acid (E) or aspartic acid (D); (g) No. 31 A.A. in the PPR motif (Mn) is isoleucine (I); and (h) No. 32 A.A. in the PPR motif (Mn) is lysine (K), arginine (R), or histidine (H). (helix A)-X-(helix B)-L formula (1).

A composition of a long-acting enzyme comprises the enzyme in a formulation comprising a buffer and an additive selected from the group consisting of tranexamic acid, ε-aminocaproic acid, and analogs of L-lysine other than tranexamic acid and ε-aminocaproic acid, combinations thereof, and mixtures thereof. The composition can further comprise another additive selected from the group consisting of L-lysine, L-arginine, L-ornithine (or its pharmaceutically acceptable salts; e.g., L-ornithine hydrochloride), γ-aminobutyric acid, 5-aminovaleric acid, 7-aminoheptanoic acid, glycylglycine, triglycine, N-α-acetyl-L-arginine, betaine, sarcosine, gelatin, HSA, streptokinase, tPA, uPA, non-ionic surfactants, glycerin, D-sorbitol, combinations thereof, and mixtures thereof. A method for prolonging the activity of an autodegradable enzyme comprises storing the enzyme after manufacture at a low pH, and reconstituting the acidified enzyme before use with a solution containing at least one of such additives. The method is useful to provide enzyme for wide use, which otherwise would lose activity upon long storage. In one embodiment the method is applicable to provide enzyme for inducing controlled posterior vitreous detachment.

The invention discloses an improved L-15 culture medium and application thereof in culturing prawn muscle cells. The improved L-15 culture medium contains 10 mmol / L of alanine, 3 mmol / L of glycine, 3 mmol / L of serine, 1.5 mmol / L of histidine, 0.5 mmol / L of lysine, 1.5 mmol / L of arginine, 1.5 mmol / L of valine, 1 mmol / L of threonine, 0.5 mmol / L of methionine, 0.5 mmol / L of leucine, 5 mmol / L of aspartic acid, 0.5 mmol / L of glutamine and 1 mmol / L of phenylalanine. The oral liquid also contains taurine, proline, glutamic acid, fetal calf serum and double antibodies, and the pH value of the oral liquid is 7.2-7.4. According to the improved L-15 culture medium, the survival rate and the adherence rate of the primary muscle cells of the penaeus vannamei boone are increased, and the growth state of the cells is improved.

The invention discloses recombinant nitrilase and an application thereof in synthesis of pharmaceutical chemicals. The recombinant nitrilase is formed by connecting a polypeptide label to the N end ofan amino acid sequence of nitrilase, uncharged glycine G is arranged at the positions of the two ends of the polypeptide label, and the rest is any one or a random combination of more of glycine G, histidine H, glutamic acid E, aspartic acid D, lysine K and arginine R. When the recombinant nitrilase is used for preparing 1-cyan cyclohexyl acetic acid, the activity is as high as 3034.7 U / g dcw, the soluble expression of the nitrilase is remarkably improved due to the introduction of the polypeptide label, the hydrolysis of 1M substrates by using a whole-cell catalyst with the same concentration is completed 30 minutes faster than that of a female parent enzyme, and the stability is superior to that of the female parent enzyme. The recombinant nitrilase disclosed by the invention can be used for catalyzing and synthesizing other medical intermediates, improving the activity of the whole-cell catalyst in the reaction, improving the solubility of other different nitrilases and improving the activity of the corresponding whole-cell catalyst.