583 results about "Threonine" patented technology

The invention discloses a formate dehydrogenase mutant and application thereof in catalytic synthesis of D-mannitol, and belongs to the technical field of bioengineering. According to the formate dehydrogenase mutant provided by the invention, the 18th-site glutamic acid of wild-type formate dehydrogenase with an amino acid sequence shown as SEQ ID NO.2 is mutated into proline, the 57th-site asparagine is mutated into glutamic acid, the 70th-site histidine is mutated into tryptophan, the 235th-site serine is mutated into threonine, and the 316th-site valine is mutated into threonine, so that the formate dehydrogenase mutant is high in enzyme activity and catalytic activity; the coenzyme circulation efficiency during the production of D-mannitol can be obviously improved, so that the yield of D-mannitol can be effectively improved. When the genetically engineered bacterium co-expressed by the formate dehydrogenase mutant and the mannitol dehydrogenase mutant is used for catalyzing 150 g / L fructose to produce D-mannitol, the yield of D-mannitol within 15 h can reach 140 g / L or above.

The invention belongs to the field of feeds, and discloses a biological feed containing a microbial microcapsule preparation and a preparation method of the biological feed. The biological feed is prepared from the following components in parts by weight: 90 to 93 parts of wall-broken rhodopseudomonas palustris powder, 2 to 3 parts of lysine hydrochloride, 0.1 to 0.5 part of methionine, 0.1 to 0.5 part of threonine, 0.3 to 1 part of arginine, 2 to 3 parts of calcium hydrophosphate, 1 to 2 parts of calcium carbonate, 0.5 to 1.2 parts of an antioxidant additive, 0.3 to 0.8 part of modified nano montmorillonite and 1 to 5 parts of a microbial microcapsule preparation. According to the biological feed, the wall-broken rhodopseudomonas palustris serves as basic nutrition and a main microorganism source of the feed and is matched with the compound probiotics of the microorganism micro-capsule preparation, the intestinal nutrition utilization rate is effectively increased, meanwhile, the antioxidant additive is added, and the problems that a single additive is narrow in function and prone to oxidation are solved; the modified nano montmorillonite is added to solve the problem of antagonism of toxin adsorption and mineral absorption.

The invention belongs to the technical field of bioengineering, and relates to a transaminase mutant, a recombinant genetically engineered bacterium and application of the transaminase mutant in catalytic synthesis of (R)-1-Boc-3-aminopiperidine.The transaminase mutant is obtained by conducting single-point or combined mutation on the 131 site and / or the 197 site of an amino acid sequence shown in SEQ ID NO.2; the mutation sites comprise that the 131 phenylalanine is mutated into aspartic acid, threonine or tyrosine, and / or the 197 lysine is mutated into arginine or leucine. Experimental results show that compared with wild type transaminase, the catalytic activity, the thermal stability and the organic solvent tolerance of the obtained mutants, especially single-point mutants MyTA1-F131Y and MyTA1-K197R and a combined mutant MyTA1-F131Y-K197R, are all remarkably improved, and compared with the wild type transaminase, the catalytic activity, the thermal stability and the organic solvent tolerance of the obtained mutants are all remarkably improved. The mutant MyTA1-F131Y-K197R can be used for efficiently catalyzing asymmetric amination of N-Boc-3-piperidone to synthesize (R)-1-Boc-3-aminopiperidine, the conversion rate of the (R)-1-Boc-3-aminopiperidine after the (R)-1-Boc-3-aminopiperidine reacts for 24 hours under the condition that the substrate concentration is 100 g / L can reach 90% or above, and the mutant MyTA1-F131Y-K197R has a good industrial application prospect.

The invention relates to a Kluyveromyces marxianus strain with high protein yield and application of the Kluyveromyces marxianus strain, which is characterized in that the Kluyveromyces marxianus strain is firstly cultured on a slant, then is transferred into a seed culture medium for seed preparation, and then is inoculated into a fermentation tank, and yeast protein is obtained by adopting index feeding; the bacterial strain is a dominant mutant strain Kluyveromyces marxianus YWX-1, the protein content in a dry thallus reaches 55% or above and is increased by 26% or above compared with that of an original bacterial strain, the bacterial strain can be used for production of single-cell protein, the essential amino acid index (EAAI) value in the protein reaches 1.2, and the bacterial strain is rich in arginine, threonine and lysine and can be applied to production of single-cell protein. These amino acids play a key role in immune regulation, intestinal mucosal barrier function and muscle protein synthesis of young animals. The YWX-1 kluyveromyces marxianus strain has a wide application prospect in the production of neoplasm protein.

The invention discloses a high-stability carbonyl reductase mutant and application of the high-stability carbonyl reductase mutant in chiral alcohol synthesis. An amino acid sequence as shown in SEQ ID NO.2 is mutated as follows: 20th leucine is replaced by any one of lysine, threonine, aspartic acid or isoleucine, and / or 55th leucine is replaced by any one of methionine, serine, lysine or isoleucine, and / or 55th leucine is replaced by any one of methionine, serine, lysine or isoleucine. Compared with a wild type enzyme, the stability of the obtained mutant is remarkably improved, particularly, single-point mutants Mut-L20I and Mut-L55I and a combined mutant Mut-L20I-L55I show excellent relative enzyme activity, thermal stability and substrate tolerance. The mutant has high catalytic activity and stability to various chiral alcohols, has the advantages of high catalytic efficiency, high thermal stability, strong substrate tolerance, easiness in fermentation production and the like, and is suitable for industrial application of enzymatic synthesis of chiral alcohols.

The present application relates to a pyridoxal kinase mutant, a recombinant expression vector and a microbial cell and their applications, and belongs to the technical field of biological catalysis. In order to solve the problem of low product concentration in existing enzyme catalysis, a pyridoxal kinase mutant is provided, the amino acid sequence is selected from the amino acid sequence shown in SEQ ID NO. 1, the lysine at position 229 is mutated to alanine, phenylalanine, methionine, arginine, threonine, histidine, serine, tyrosine, valine, leucine, isoleucine, proline, asparagine, aspartic acid or glutamic acid; the pyridoxal kinase mutant is used for catalyzing pyridoxal to synthesize pyridoxal phosphate, and a recombinant expression vector and a microbial cell can be further formed. The present application has good enzyme activity, high product conversion rate, high concentration of pyridoxal phosphate obtained, and the concentration of the product catalyzed by the wild-type pyridoxal kinase to phosphorylate pyridoxal is obviously improved.

In the first aspect, the present disclosure provides a Lactoferrin polypeptide fragment, where the Lactoferrin polypeptide fragment has an amino acid sequence shown in SEQ ID NO: 1. In the second aspect, the present disclosure provides a preparation method of the Lactoferrin polypeptide fragment, including: protecting amino acids using a 9-fluorenylmethoxycarbonyl (Fmoc) protecting group, coupling the amino acids with a P-hydroxymethylphenoxymethyl polyethylene resin (HMP resin) in an order of cysteine, alanine, leucine, cysteine, glutamate, threonine, asparagine, aspartate, asparagine, phenylalanine, leucine, leucine, asparagine, and lysine, and separating the HMP resin to obtain a target Lactoferrin polypeptide fragment. In the third aspect, the present disclosure further provides an anti-Lactoferrin antibody prepared using the Lactoferrin polypeptide fragment, and use of the Lactoferrin polypeptide fragment in preparation of an anti-Lactoferrin flow cytometric antibody and in preparation of a Lactoferrin detection product.

The invention discloses application of copper-amino acid nano enzyme in preparation of anti-inflammatory drugs, and relates to the technical field of biomedical new materials, amino acids comprise glycine, arginine, histidine, threonine, phenylalanine and cysteine; the ratio of the amino acid to the copper ions is 1: (0.5-5), and the synthesis temperature of the copper-cysteine nano enzyme is 25-125 DEG C. The copper-amino acid nano-enzyme library established by the invention has efficient hydroxyl free radical, superoxide free radical and hydrogen peroxide scavenging activity; wherein the copper-cysteine nano-enzyme shows the highest enzymatic activity, and shows low toxicity and good biocompatibility in both the cell level and the animal level; meanwhile, the copper-cysteine nano-enzyme also shows anti-inflammatory activity and anti-oxidative stress activity, can remarkably improve cell inflammation and body inflammation, relieves and treats dextran sodium sulfate induced mouse ulcerative colitis, and can be further applied to preparation of drugs for treating inflammatory bowel diseases.

The invention relates to a method for improving fermentation production efficiency of bacillus subtilis lipopeptide sodium by controlling threonine flow acceleration rate based on fermentation process oxygen uptake rate curve feedback. Bacillus subtilis is used as a production strain, and lipopeptide sodium is produced through deep liquid state fermentation. In the fermentation process, the oxygen uptake rate of the process is detected, a threonine and ammonium sulfate continuous feeding control process based on oxygen uptake rate curve parameters is implemented, the oxygen uptake rate in the fermentation process is stably maintained to be 60-65 mmo1 / L / h, the ammonium ion concentration is maintained to be 15-20 mmol / L, and rapid growth of hyphae and rapid increase of the lipopeptide sodium synthesis rate can be achieved. The threonine and ammonium sulfate fed-batch control process based on oxygen uptake rate feedback control is established, the production period is shortened, and the fermentation production level is stably improved.

The invention provides an SNP (Single Nucleotide Polymorphism) marker for targeted identification of systemic lupus erythematosus of children and application of the SNP marker. A new SNP site (RS25671007) is identified in a child systemic lupus erythematosus patient through whole exon sequencing, the site is located at the 734th pair of basic groups of a PABPC3 gene, and mutation from C to T exists at the site, or mutation from threonine to isoleucine exists in coded amino acid. In addition, in-vitro cell model experiments prove that the SNP causes significant up-regulation of the antibody type transformation function, and the SNP can be used as a reference marker for risk stratification or medication guidance of early targeted diagnosis, detection, gene evaluation and the like of systemic lupus erythematosus of children.

The invention relates to a carbonyl reductase mutant based on cosubstrate catalytic ability optimization and application thereof, the mutant is constructed on the basis of a carbonyl reductase BaSDRX amino acid sequence as shown in SEQ ID No.2, the nucleotide sequence of the carbonyl reductase is as shown in SEQ ID No.1 in a sequence table, and the nucleotide sequence of the carbonyl reductase is as shown in SEQ ID No.2 in the sequence table. The mutant is single-point mutation or multi-point combined mutation on the basis of an amino acid sequence of carbonyl reductase BaSDRX as shown in SEQ ID No.2: threonine Thr133 at the 133 site, arginine Arg137 at the 137 site and glutamic acid Glu142 at the 142 site; when the mutant enzyme or a recombinant cell containing the mutant enzyme is applied to synthesis of (S)-1-(2, 6-difluorophenyl) ethanol through asymmetric reduction of 2, 6-difluoroacetophenone, high catalytic activity and high stereoselectivity are achieved, and high-optical-purity (S)-1-(2, 6-difluorophenyl) ethanol (eet; therefore, the method has a good industrial application and development prospect.

The invention relates to the technical field of bioengineering, in particular to a penicillin G acylase mutant, polynucleotide, an expression vector and application. The penicillin G acylase mutant is obtained by carrying out site-directed mutagenesis on a wild type penicillin G acylase gene of parent Escherichia coli, and carrying out site-directed mutagenesis on the wild type penicillin G acylase gene to obtain the penicillin G acylase mutant. Phenylalanine (F) at the 24th site of an alpha chain, proline (P) at the 383rd site of a beta chain, threonine (T) at the 384th site of the beta chain, glutamic acid (G) at the 385th site of the beta chain and serine (S) at the 386th site of the beta chain of the penicillin G acylase are introduced and mutated by a whole plasmid PCR (Polymerase Chain Reaction) technology to obtain mutants. When the penicillin G acylase mutant obtained by the invention is used for catalyzing methyl mandelate and 3-(1-methyl-1H-tetrazole-5-yl) thiomethyl-7-aminocephalosporanic acid to synthesize cefamandole, the synthesis activity is improved, and meanwhile, the side reaction rate is greatly reduced.

The present invention relates to the fields of agriculture, plant biotechnology, and molecular biology. Specifically, the present invention relates to a wheat EPSPS mutant protein and use thereof in improving the tolerance of wheat to glyphosate. The mutant protein comprises an amino acid sequence having the following mutations compared to the EPSPS amino acid sequence of any genome of wild-type wheat: in the amino acid sequence set forth in SEQ ID NO: 2, the amino acid at position 168 is mutated from threonine to isoleucine, the amino acid at position 169 is mutated from alanine to valine, and the amino acid at position 172 is mutated from proline to serine. The mutant protein enables the production of stable glyphosate-resistant wheat, showing important significance for wheat breeding.

There is provided a Bronstinan protein variant comprising X1 X2 KCKX6 X7 YX9 NYPX13 X14 KCX17 X18 AX20 QCNYDCKLDKHARX34 GECFYDEX42 RNX45X46 CX48 CDYCX53YX55 (SEQ ID NO: 1) wherein X1, X20 and X47 are each independently an amino acid having a polar uncharged side chain, X2 is an amino acid having a negatively charged side chain, X6 is glutamine (E) or an amino acid having a positively charged side chain, X7, X13, X18, X45 and X48 are each independently an amino acid having a hydrophobic side chain, X7, X13, X18, X45 and X48 are each independently an amino acid having a hydrophobic side chain, X7, X13, X18 X17 is lysine (K) or an amino acid having a polar uncharged side chain, X14 is arginine (R) or an amino acid having a polar uncharged side chain, X9 is arginine (R) or an amino acid having a negatively charged side chain, X42 is an amino acid having a positively charged side chain, X34 is alanine or an amino acid having a polar uncharged side chain, X17 is lysine (K) or an amino acid having a polar uncharged side chain, X14 is arginine (R) or an amino acid having a polar uncharged side chain. X46 is an amino acid having a polar uncharged side chain, X53 is glutamic acid, glutamine or lysine, and X55 is proline, arginine, threonine or no residue. Also disclosed are polynucleotides encoding the bristinin variants, cells expressing the bristinin variants, and methods of making the bristinin variants.

The invention discloses a monoclonal antibody which is specifically combined with a microtubule associated protein tau (microtubule associated protein with 217 Thrphorylation, pTau217) of which the 217 site is phosphorylated by threonine, and a preparation method of the monoclonal antibody. The invention provides an amino acid sequence of a variable domain of the monoclonal antibody, and an amino acid sequence of a complementary determining region (CDR) contained in the amino acid sequence of the variable domain of the monoclonal antibody. The monoclonal antibody disclosed by the invention has the capability of specifically recognizing and remarkably combining pTau217, and can be used for developing and producing pTau217 clinical in vitro diagnosis (IVD) medical equipment products based on an immunological detection principle as a reagent raw material.

An Fc-binding polypeptide with improved alkaline stability comprising a mutant of the Fc-binding domain of Staphylococcus protein A (SpA), said mutant being defined by SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 22, SEQ ID NO 51 or EQ ID NO 52, wherein at least the asparagine or serine residue at a position corresponding to position 11 in SEQ ID NO: 4-7 has been mutated to an amino acid selected from the group consisting of glutamic acid, lysine, tyrosine, threonine, phenylalanine, leucine, isoleucine, tryptophan, methionine, valine, alanine, histidine and arginine.

The invention relates to a protein consisting of an amino acid sequence in which at least one modification selected from the group consisting of the following [1] to [7] is introduced in the amino acid sequence represented by SEQ ID NO: 1: [1] a modification in which the amino acid residue at a position 103 is substituted with a lysine residue, [2] a modification in which the amino acid residue at a position 76 is substituted with a cysteine residue, [3] a modification in which the amino acid residue at a position 144 is substituted with a cysteine residue, [4] a modification in which the amino acid residue at a position 134 is substituted with a glycine residue, [5] a modification in which the amino acid residue at a position 222 is substituted with a methionine residue, [6] a modification in which the amino acid residue at a position 73 is substituted with a glutamine residue, and [7] a modification in which the amino acid residue at a position 203 is substituted with a threonine residue.

The invention provides a moulting feed for laying hens and an artificial moulting method for quickly recovering high yield, and the moulting feed for laying hens comprises the following raw materials in parts by mass: 7-8 parts of Chinese prickly ash seeds, 20-22 parts of crude protein feed, 0.5-2 parts of yeast culture, 2-4 parts of threonine residues, 8-10 parts of calcium-containing supplement, 0.1-1 part of soybean oil, 50-65 parts of corn and 2-3 parts of LD625. Wherein the content of crude protein is 15%-16%, and the content of calcium is 3%-4.0%. The specific formula of the laying hen moulting feed is optimally designed, and the illumination intensity and time in the moulting process are regulated and controlled, so that the second laying rate can quickly reach the peak and the second laying peak lasts for a long time after primary artificial moulting, and the laying rate of laying hens can reach the peak after secondary artificial moulting. The third-time egg laying rate can quickly reach the peak, the duration time of the third-time egg laying peak is long, the continuous and excellent egg laying effect is achieved, the moulting cost is reduced, the breeding period is prolonged, and application and popularization are facilitated.

The application relates to the technical field of beef cattle breeding, and particularly discloses a compound preparation for promoting the feed intake, daily weight gain and improving the meat quality of beef cattle and application thereof, which is prepared from the following components in percentage by volume: 40% of micro-ecological preparation, 30% of hawthorn, 10% of medicated leaven, 10% of malt, 5% of areca nut and 5% of dried tangerine or orange peel; the compound preparation is prepared from microorganisms and multiple natural Chinese herbal medicines in a specific and scientific matching ratio; experiments prove that the compound preparation can increase the feed intake of beef cattle by 11.33%, increase the daily weight gain by 16.16%, and significantly shorten the breeding cycle; meanwhile, the contents of aspartic acid, threonine, glutamic acid, alanine, valine, isoleucine, leucine, tyrosine, phenylalanine, lysine, arginine and proline in the muscle are significantly increased, the nutritional quality and flavor taste of beef are effectively improved, the preparation is natural, residue-free and side-effect-free, the preparation method is simple, the cost is low, and the preparation has extremely high practical value and popularization prospect.

The invention discloses laying hen feed immune peptide and a preparation method thereof, and belongs to the technical field of laying hen feed additives. The immune peptide is prepared from the following raw materials in percentage by mass: 29% of threonine, 25% of chili meal, 20% of Chinese prickly ash seeds and 26% of Chinese prickly ash leaf powder. The preparation method comprises the following steps: respectively crushing the raw materials until the particle size is 0.3-0.8 mm, mixing the zanthoxylum bungeanum seed powder, the pepper meal powder and the zanthoxylum bungeanum leaf powder in sequence, and then adding the threonine powder, and mixing for 25-30 minutes to obtain a finished product. The feed has the core advantages that by utilizing the synergistic effect of natural active ingredients in the threonine, the pepper meal, the Chinese prickly ash seeds and the Chinese prickly ash leaf powder, the immune function of laying hens is remarkably enhanced, the morbidity is reduced, meanwhile, the laying rate of the laying hens, the eggshell quality and the egg nutritional value are improved, and the raw materials are natural, free of residues and high in safety.

The invention relates to the field of enzyme engineering, and discloses a sandalene synthase mutant, a preparation method and application thereof, the sandalene synthase mutant comprises one of a sandalene synthase mutant Q33A, a sandalene synthase mutant T34A, a sandalene synthase mutant K133A and a sandalene synthase mutant F452A, and the sandalene synthase mutant is one of the sandalene synthase mutant Q33A, the sandalene synthase mutant T34A and the sandalene synthase mutant F452A. The mutant is obtained by mutating threonine at the 34th position of wild-type santalene synthase into alanine, glutamine at the 33rd position of wild-type santalene synthase into alanine, lysine at the 133rd position of wild-type santalene synthase into alanine and phenylalanine at the 452nd position of wild-type santalene synthase into alanine. The yield of alpha-alkene synthase produced by fermentation of genetically engineered bacteria prepared by transforming the mutant into saccharomycetes is 0.35-2.24 times that of wild santalene synthase.

The invention discloses a generalized pustular psoriasis diagnosis marker based on metabonomics and application of the generalized pustular psoriasis diagnosis marker. The diagnostic marker is prepared from one or more of the following 35 compounds: pyruvic acid, alpha-ketoisovaleric acid, 2-hydroxybutyric acid, 3-hydroxybutyric acid, methane thiophosphoric acid, proline, uracil, tranexamic acid, 4-aminobutyric acid, threonine, scopoletin, dodecanol, N-methyl-L-leucine, L-cysteine-glycine and L-kynurenine. The feed additive is prepared from the following raw materials: 3-hydroxybenzoic acid, allantoin, delta-tocopherol, xylofuranose, glucose-1-phosphoric acid, pyrophosphate, taurine, L-asparagine, phthalic acid, 4-(dimethylamino) azobenzene, 5-tert-butyl-1h-indole-2, 3-dione, quinic acid, glucose, histidine, lysine, palmitic acid, 7-methylguanine, oleic acid and whale acid. The marker can be used for accurately distinguishing patients with generalized pustular psoriasis from healthy people.

The present invention provides a therapeutic agent for sepsis and / or septic shock, comprising, as an active ingredient, a compound capable of suppressing phosphorylation of threonine at position 749 in human STAT1; a method for screening for a candidate compound serving as an active ingredient of a therapeutic agent for sepsis and / or septic shock, the method comprising selecting a compound capable of suppressing phosphorylation of threonine at position 749 in human STAT1; a therapeutic agent for colitis, comprising, as an active ingredient, a compound capable of promoting phosphorylation of threonine at position 749 in human STAT1; a method for screening for a candidate compound serving as an active ingredient of a therapeutic agent for colitis, the method comprising selecting a compound capable of promoting phosphorylation of threonine at position 749 in human STAT1; a therapeutic agent for systemic lupus erythematosus, comprising, as an active ingredient, a compound capable of inhibiting human STAT1; and a method for screening for a candidate compound serving as an active ingredient of a therapeutic agent for systemic lupus erythematosus, the method comprising selecting a compound capable of inhibiting human STAT1.

The present invention discloses a method for synthesizing hydroxytyrosol by multi-enzyme cascade, comprising: 1) preparing a hydroxytyrosol product by using 3,4-dihydroxybenzaldehyde, L-threonine, sodium formate, NAD + As raw material, L-threonine transaldolase, alcohol dehydrogenase, and formate dehydrogenase are used to catalyze the synthesis of L-threo-3-(3,4-dihydroxyphenyl)serine; 2) L-threo-3-(3,4-dihydroxyphenyl)serine is used as substrate, glucose, NAD + Hydroxytyrosol is synthesized through a cascade catalysis of phenylserine dehydratase, α-ketoacid decarboxylase, aldehyde reductase, and glucose dehydrogenase. The synthesis method provided by the present invention achieves a hydroxytyrosol yield of >99% and a space-time yield of 0.88 g / L / h, currently the highest, showing great potential for industrial application and suitable for further promotion and application.

The invention discloses application of a TREX1 protein non-substrate DNA binding interface as a target spot in preparation of an immunoregulation medicine, and relates to the technical field of biological medicines. Wherein the TREX1 protein is a human source TREX1 protein, and the non-substrate DNA binding interface comprises threonine at the 49th site of the TREX1 protein, arginine at the 211th site of the TREX1 protein, glutamine at the 213th site of the TREX1 protein and arginine at the 217th site of the TREX1 protein. The non-substrate DNA binding interface in the TREX1 is found for the first time, the key function of the non-substrate DNA binding interface in maintaining immune homeostasis and tumor immune escape is defined through mutation verification and functional analysis, and a new anti-tumor immune strategy with the non-substrate DNA binding interface as a target spot is provided. The discovery not only makes up the blank of TREX1 structure research, but also provides a new theoretical basis and a drug development direction for immune regulation molecule design.

The present disclosure can improve the degree of soy protein proteolysis and the ability to produce valine, isoleucine, and leucine, which are branched-chain amino acids, as well as other amino acids, such as threonine, glycine, tyrosine, and lysine. Accordingly, the present disclosure can prevent sarcopenia and has antioxidant activity. Also, the present disclosure can maintain protein metabolic balance and relieve sarcopenia by muscle synthesis.The self-aggregation, hydrophobicity, and intestinal adhesion of a mixed strain is improved compared to a case where a single strain used for the mixed strain is used. Therefore, when the mixed strain of the present disclosure is ingested, the strain can remain for a long time in the intestine.

The present invention relates to an antibody or binding fragment thereof that binds to a protein, preferably a T cell receptor, comprising an epitope comprising or consisting of an amino acid sequence having at least 80 %, such as 83 %, preferably at least 90 %, for instance 100 % sequence identity to the amino acid sequence set forth in SEQ ID NO: 62 (EVPKXiR), wherein Xi is selected from Alanine (A), Arginine (R), Asparagine (N), Aspartic acid (D), Cysteine (C), Glutamine (Q), Glutamic acid (E), Glycine (G), Histidine (H), Isoleucine (I), Leucine (L), Lysine (K), Methionine (M), Phenylalanine (F), Proline (P), Serine (S), Threonine (T), Tryptophan (W), Tyrosine (Y), Valine (V). Further, the invention relates to pharmaceutical compositions comprising such an antibody or binding fragment thereof and to the use of such an antibody or binding fragment thereof for use as a medicament or for use as a screening agent.

To provide a human interferon-beta mutant having a double mutation and a method for improving the safety of the human interferon-beta mutant.SOLUTION: Provided are a human interferon-beta variant comprising an amino acid sequence in which the 17th amino acid cysteine of human interferon-beta is substituted with serine and the 27th amino acid arginine is substituted with threonine, and a method for improving the stability of a human interferon-beta R27T variant, the method comprising the step of changing the 17th amino acid cysteine of a human interferon-beta R27T variant, in which the 27th amino acid arginine of human interferon-beta is substituted with threonine, to serine.SELECTED DRAWING: Figure 1

To provide an improved antibody-drug conjugate and a pharmaceutical composition containing the antibody-drug conjugate.SOLUTION: The invention is based on the concept that it is possible to generate antibodies that exhibit improved potency (e.g., one or more of increased (e.g., detectable increase) toxin release in target mammalian cells, increased (e.g., detectable increase) killing of target mammalian cells, and increased (e.g., detectable increase) endolysosomal delivery). In some embodiments of any of the antibodies described herein, the heavy chain CH1 - CH2 - CH3 sequence consisting of the specific sequence comprises a substitution of lysine to cysteine at amino acid position 105 and a deletion of threonine at amino acid positions 106 and 108.SELECTED DRAWING: None

This invention discloses a hair repair composition for permed hair, comprising, by weight: 0.02-1.0 parts hydrolyzed plant protein, 0.1-2.0 parts biomimetic amino acid complex, 50-95 parts carrier, and 0.5-15 parts additives. The hydrolyzed plant protein is obtained from Moringa seed protein through multi-enzyme synergistic hydrolysis, with a molecular weight less than 3500 Daltons. The biomimetic amino acid complex includes at least wheat amino acids, soybean amino acids, arginine hydrochloride, serine, and threonine. Under weakly acidic conditions, this composition can simultaneously repair broken disulfide bonds, hydrogen bonds, and ionic bonds in hair. The hydrolyzed plant protein provides disulfide bond reconnection sites, and the biomimetic amino acid complex constructs a multi-point weak bond network through hydroxyl and ionic groups, achieving "triple bond repair" synergistically. This invention can significantly improve the mechanical strength, elasticity, and breakage resistance of damaged hair, with long-lasting, gentle, and safe repair effects, suitable for daily care of damaged hair after perming and dyeing.