Abstract: A semiconductor device and a method for manufacturing the same are provided in this disclosure. The semiconductor device includes a semiconductor heterostructure layer. The semiconductor heterostructure layer includes alternating first semiconductor material layers and second semiconductor material layers. Two-dimensional electron gas (2DEG) may be generated between each first semiconductor material layer and adjacent second semiconductor material layer. A conductive structure, including a plurality of conductive fingers extends from a surface of the semiconductor heterostructure layer into the semiconductor heterostructure layer. The plurality of conductive fingers are arranged in a direction substantially parallel to the surface. The lengths of the plurality of conductive fingers progressively increase in that direction so that an end portion of each conductive finger is respectively positioned in a different second semiconductor material layer and is not in contact with the 2DEG.

Abstract: The present disclosure relates to a semiconductor device and a manufacturing method thereof. The semiconductor device includes a semiconductor heterostructure layer and a conductive structure. The semiconductor heterostructure layer includes alternating first semiconductor material layers and second semiconductor material layers. 2DHGs may be generated between each first semiconductor material layer and adjacent second semiconductor material layer. The conductive structure includes a plurality of conductive fingers extending from a surface of the semiconductor heterostructure layer into the semiconductor heterostructure layer. The plurality of conductive fingers are arranged in a direction substantially parallel to the surface. The lengths of the plurality of conductive fingers progressively increase in that direction, so that an end portion of each conductive finger is respectively positioned in a different second semiconductor material layer and is not in contact with the 2DHG.

Abstract: The present invention discloses novel proinsulin glargine and method for for preparing insulin glargine therefrom. A sequence of the proinsulin glargine containing SOD fusion peptide subjected to site-directed mutagenesis and “0 C peptide” is designed; recombinant Escherichia coli for expressing insulin glargine are constructed; insulin glargine fusion protein in a form of an inclusion body is expressed; and denaturation, renaturation, modification, enzyme digestion, separation and purification are carried out to obtain a mature insulin glargine active pharmaceutical ingredient. According to the present invention, the SOD fusion peptide sequence is mutated to enhance the fermentation yield of the insulin glargine by 75%; and a “0 C peptide” strategy is adopted to reduce the quality loss and miscleavage impurities in the enzyme digestion transformation. The purity of the insulin glargine active pharmaceutical ingredient prepared in the present invention is up to 99.

Abstract: The invention relates to a low molecular weight sulfate chondroitin and a preparation method thereof. A low molecular weight chondroitin sulfate with the average molecular weight of less than 1000 Dalton can be obtained by a production process of chondroitin sulfate lyase degradation, deproteinization, filtration and sterilization and drying using macromolecular sulfate chondroitin as a raw material. The low molecular weight Chondroitin sulfate has a narrow molecular weight distribution range, the ratio of chondroitin sulfate disaccharide is 43˜60% and the ratio of chondroitin sulfate tetrasaccharide is 30˜45%, the sum of chondroitin sulfate disaccharide and chondroitin sulfate tetrasaccharide is more than 87%, the total oligosaccharide content of low molecular weight chondroitin sulfate is more than 97% and the protein content is less than 0.

Abstract: Provided are chondrosulfatase and a use thereof, belonging to the technical field of biological engineering. Chondrosulfatase is screened and identified from the natural world, the maximum similarity between its amino acid sequence and that of the chondrosulfatase reported by NCBI being 85%; then the expression in Escherichia coli and Bacillus subtilis is optimized, achieving the high-efficiency biosynthesis of chondrosulfatase having high enzymatic activity, the maximum enzyme activity being 11976.5 U/L; furthermore, the entire process and post-processing are simpler. The invention has potentially broad value in application in the preparation of products containing low molecular-weight chondroitin sulfate in the fields of medicine, cosmetics, and biology, lays the foundation for efficient fermentation of a microbial system to produce a chondrosulfatase having high enzyme activity, and is suitable for industrialized production applications.

Abstract: The invention relates to a low molecular weight sulfate chondroitin and a preparation method thereof. A low molecular weight chondroitin sulfate with the average molecular weight of less than 1000 Dalton can be obtained by a production process of chondroitin sulfate lyase degradation, deproteinization, filtration and sterilization and drying using macromolecular sulfate chondroitin as a raw material. The low molecular weight Chondroitin sulfate has a narrow molecular weight distribution range, the ratio of chondroitin sulfate disaccharide is 43˜60% and the ratio of chondroitin sulfate tetrasaccharide is 30˜45%, the sum of chondroitin sulfate disaccharide and chondroitin sulfate tetrasaccharide is more than 87%, the total oligosaccharide content of low molecular weight chondroitin sulfate is more than 97% and the protein content is less than 0.

Abstract: The invention belongs to the technical field of polypeptide preparation methods, and in particular relates to a high-purity ACTH (human sequence) or analogue and large-scale preparation method thereof. The main steps include: amino acids are coupled from the C-terminal to the N-terminal by Fmoc solid-phase synthesis method to obtain the crude ACTH (human sequence) or analogue peptidyl-resin with protective groups, wherein the reaction temperature of C-15 peptide synthesis is 40-60° C. After cleavage and precipitation, the crude product of ACTH (human sequence) or analogue is obtained, and then the high-purity product is obtained by liquid chromatography. The chromatographic purity of ACTH (human sequence) or analogue prepared by the invention is more than 99%, the stability is good, and the yield of the target peptide is ?63%.

Abstract: A macromolecular hyaluronic acid is used as a raw material, and is subjected to production processes such as hyaluronidase hydrolysis, heating and inactivation, activated carbon filtration, and spray and dry to obtain an ultra-low molecular weight hyaluronic acid product having an average molecular weight of less than 1200 Da. The product is a mixture of hyaluronic acid disaccharide to dodecaose. The content of hyaluronic acid disaccharide is 5-40%. The content of hyaluronic acid tetrasaccharide is 40-70%. The content of hyaluronic acid hexasaccharide is 10-30%. The content of hyaluronic acid octasaccharide is 1-15%. The content of hyaluronic acid decaose is 1-10%. The content of that higher than hyaluronic acid decaose is less than 6%. Compared with other available low molecular hyaluronic acid, the product has a more significant permeation, moisturizing, and repair promotion capability, and can be widely used in fields of medical products, health care products, cosmetics and the like.

Abstract: The invention belongs to the technical field of polypeptide preparation methods, and in particular relates to a high-purity ACTH (human sequence) or analogue and large-scale preparation method thereof. The main steps include: amino acids are coupled from the C-terminal to the N-terminal by Fmoc solid-phase synthesis method to obtain the crude ACTH (human sequence) or analogue peptidyl-resin with protective groups, wherein the reaction temperature of C-15 peptide synthesis is 40-60° C. After cleavge and precipitation, the crude product of ACTH (human sequence) or analogue is obtained, and then the high-purity product is obtained by liquid chromatography. The chromatographic purity of ACTH (human sequence) or analogue prepared by the invention is more than 99%, the stability is good, and the yield of the target peptide is ?63%.

Abstract: Provided are chondrosulfatase and a use thereof, belonging to the technical field of biological engineering. Chondrosulfatase is screened and identified from the natural world, the maximum similarity between its amino acid sequence and that of the chondrosulfatase reported by NCBI being 85%; then the expression in Escherichia coli and Bacillus subtilis is optimized, achieving the high-efficiency biosynthesis of chondrosulfatase having high enzymatic activity, the maximum enzyme activity being 11976.5 U/L; furthermore, the entire process and post-processing are simpler. The invention has potentially broad value in application in the preparation of products containing low molecular-weight chondroitin sulfate in the fields of medicine, cosmetics, and biology, lays the foundation for efficient fermentation of a microbial system to produce a chondrosulfatase having high enzyme activity, and is suitable for industrialized production applications.

Abstract: The invention relates to a low molecular weight sulfate chondroitin and a preparation method thereof. A low molecular weight chondroitin sulfate with the average molecular weight of less than 1000 Dalton can be obtained by a production process of chondroitin sulfate lyase degradation, deproteinization, filtration and sterilization and drying using macromolecular sulfate chondroitin as a raw material. The low molecular weight Chondroitin sulfate has a narrow molecular weight distribution range, the ratio of chondroitin sulfate disaccharide is 43˜60% and the ratio of chondroitin sulfate tetrasaccharide is 30˜45%, the sum of chondroitin sulfate disaccharide and chondroitin sulfate tetrasaccharide is more than 87%, the total oligosaccharide content of low molecular weight chondroitin sulfate is more than 97% and the protein content is less than 0.

Abstract: Provided in the present invention are a novel pro-insulin aspart structure design and a method for preparing insulin aspart. The main steps comprise designing the pro-insulin aspart sequence, constructing recombinant insulin aspart engineered bacteria, inducing an insulin fusion protein expressed in the form of an inclusion body by means of the engineered bacteria, and obtaining a mature insulin aspart material drug by means of denaturing, renaturing enzymatic digestion, and separation purification, By means of changing the recombinant leading peptide and C-peptice sequences, the invention avoids the dangerous and tedious step of cleavage using cyanogen bromide. The C-peptide is shortened to one amino acid, reducing the quality loss of enzymatic digestion conversion.

Abstract: The invention belongs to the technical field of polypeptide preparation methods, and in particular relates to a preparation method of a liraglutide intermediate polypeptide GLP-1 (7-37). In the preparation method, main steps include constructing recombinant liraglutide engineered bacteria via E. coli to induce expression of a liraglutide intermediate fusion protein in the form of inclusion bodies, and performing denaturation, renaturation, enzyme digestion, separation and purification to obtain the liraglutide intermediate polypeptide GLP-1 (7-37). The invention alters expression pattern into the expression of the intracellular insoluble inclusion bodies by changing a signal peptide of the recombinant sequence to increase significantly expression level. The liraglutide intermediate polypeptide prepared by the invention has a purity up to 87% or more and a yield of more than 85%.

Abstract: A method of resolving a racemic mixture of (±)-Huperzine A to (?)-Huperzine A includes: separating the (?)-Huperzine A from the racemic mixture of (±)-Huperzine A by chiral high performance liquid chromatography (HPLC), the chiral HPLC being performed utilizing a mobile phase including a solution including an alcohol and one selected from dichloromethane, trichloromethane, and a mixture thereof, and the chiral HPLC being performed utilizing a chiral stationary phase including a polysaccharide derivative.

Abstract: Disclosed is a preparation method for a racemic adrenaline as represented by formula II. The method comprises the following steps: compound 1 is directly racemized in an acidic solution to produce compound 2, the acid solution comprising neither sodium bisulfite nor salicylic acid; and specifically comprises (a), in the acid solution of which the pH is 0.5-1.5, compound 1 is placed under the protection of nitrogen gas and, with the reaction temperature being controlled at 75-95° C., stirred and reacted for 1-3 hours; (b) the reaction solution is controlled at a temperature of 5-20° C., into which an activated carbon is added, under the protection of nitrogen gas, stirred for 20-40 minutes, and filtered, then a filtrate is collected; the filtrate is controlled at a temperature of 5-20° C., the pH thereof is adjusted using ammonia to 8.5-9.5, and is filtered when the pH is stabilized, and a filter cake is washed and dried to produce a high purity racemic adrenaline white powder.

Abstract: A preparation method for a racemic adrenaline as represented by formula II. The method may comprise the following steps: compound 1 is directly racemized in an acidic solution to produce compound 2, the acid solution comprising neither sodium bisulfite nor salicylic acid; and specifically comprises (a), in the acid solution of which the pH is 0.5-1.5, compound 1 is placed under the protection of nitrogen gas and, with the reaction temperature being controlled at 75-95° C., stirred and reacted for 1-3 hours; (b) the reaction solution is controlled at a temperature of 5-20° C., into which an activated carbon is added, under the protection of nitrogen gas, stirred for 20-40 minutes, and filtered, then a filtrate is collected; the filtrate is controlled at a temperature of 5-20° C., the pH thereof is adjusted using ammonia to 8.5-9.5, and is filtered when the pH is stabilized, and a filter cake is washed and dried to produce a high purity racemic adrenaline white powder.

Abstract: The invention belongs to the technical field of polypeptide preparation methods, and in particular relates to a preparation method of a liraglutide intermediate polypeptide GLP-1 (7-37). In the preparation method, main steps include constructing recombinant liraglutide engineered bacteria via E. coli to induce expression of a liraglutide intermediate fusion protein in the form of inclusion bodies, and performing denaturation, renaturation, enzyme digestion, separation and purification to obtain the liraglutide intermediate polypeptide GLP-1 (7-37). The invention alters expression pattern into the expression of the intracellular insoluble inclusion bodies by changing a signal peptide of the recombinant sequence to increase significantly expression level. The liraglutide intermediate polypeptide prepared by the invention has a purity up to 87% or more and a yield of more than 85%.

Abstract: A method of resolving a racemic mixture of (±)-Huperzine A to (?)-Huperzine A includes: separating the (?)-Huperzine A from the racemic mixture of (±)-Huperzine A by chiral high performance liquid chromatography (HPLC), the chiral HPLC being performed utilizing a mobile phase including a solution including an alcohol and one selected from dichloromethane, trichloromethane, and a mixture thereof, and the chiral HPLC being performed utilizing a chiral stationary phase including a polysaccharide derivative.

Abstract: A method of resolving a racemic mixture of (±)-Huperzine A to (?)-Huperzine A includes: separating the (?)-Huperzine A from the racemic mixture of (±)-Huperzine A by chiral high performance liquid chromatography (HPLC), the chiral HPLC being performed utilizing a mobile phase including a solution including an alcohol and one selected from dichloromethane, trichloromethane, and a mixture thereof, and the chiral HPLC being performed utilizing a chiral stationary phase including a polysaccharide derivative.

Abstract: A method for the purification of idraparinux sodium includes: passing a solution including a crude idraparinux sodium through a column including a sodium ion exchange resin to obtain a first mixture; passing a solution including the first mixture through a gel chromatogaphy column to obtain a second mixture; and precipitating a purified idraparinux sodium from a solution including the second mixture.