摘要:
Disclosed is a method for the mass production of a monomeric or dimeric immunoglobulin Fc region, free of initial methionine residues, using a recombinant expression vector comprising a nucleotide sequence coding for a recombinant immunoglobulin Fc region comprising an immunoglobulin Fc region linked at the N-terminus thereof to an immunoglobulin Fc region via a peptide bond.
摘要:
Disclosed is a method for the mass production of a monomeric or dimeric immunoglobulin Fc region, free of initial methionine residues, using a recombinant expression vector comprising a nucleotide sequence coding for a recombinant immunoglobulin Fc region comprising an immunoglobulin Fc region linked at the N-terminus thereof to an immunoglobulin Fc region via a peptide bond.
摘要:
A modified human granulocyte-colony stimulating factor (hG-CSF) is produced by culturing a microorganism transformed with an expression vector comprising a gene encoding a modified hG-CSF to produce and secrete the modified hG-CSF to periplasm, said modified hG-CSF being obtained by replacing at least one of the 1st, 2nd, 3rd and 17th amino acids of wild-type hG-CSF (SEQ ID NO: 2) with other amino acid
摘要翻译:通过培养用包含编码修饰的hG-CSF的基因的表达载体转化的微生物来产生修饰的人粒细胞集落刺激因子(hG-CSF),以产生和分泌经修饰的hG-CSF至周质,所述修饰的hG-CSF 通过将野生型hG-CSF(SEQ ID NO:2)的第1,第2,第3和第17氨基酸中的至少一个替换为其他氨基酸而获得
摘要:
A heterologous protein is produced by: (i) culturing a microorganism transformed with an expression vector comprising a gene encoding a modified E. coli enterotoxin II signal peptide fused with the heterologous protein to produce and secrete the heterologous protein to periplasm, the modified E. coli enterotoxin II signal peptide being obtained by replacing at least one of the 2nd, 4th, 5th, 12th, 20th, and 22nd amino acids of E. coli enterotoxin II signal peptide of the following amino acid sequence (SEQ ID NO: 1) with another amino acid, with the proviso that at least one of the 2nd and 4th amino acid of the modified peptide is lysine; and (ii) recovering the heterologous protein from the periplasm.
摘要翻译:通过以下方式产生异源蛋白质:(i)培养用包含编码与异源蛋白质融合的修饰的大肠杆菌肠毒素II信号肽的基因的表达载体转化的微生物,以产生和分泌异源蛋白质至周质,修饰的E. 通过将下述氨基酸序列(SEQ ID NO:1)的大肠杆菌肠毒素II信号肽的第2,第4,第5,第12,第20和第22氨基酸中的至少一个替换为大肠杆菌肠毒素II信号肽, 另一氨基酸,条件是修饰肽的第二和第四氨基酸中的至少一个是赖氨酸; 和(ii)从周质中回收异源蛋白质。
摘要:
A modified human granulocyte-colony stimulating factor (hG-CSF) is produced by culturing a microorganism transformed with an expression vector comprising a gene encoding a modified hG-CSF to produce and secrete the modified hG-CSF to periplasm, said modified hG-CSF being obtained by replacing at least one of the 1st, 2nd, 3rd and 17th amino acids of wild-type hG-CSF (SEQ ID NO: 2) with other amino acid.
摘要翻译:通过培养用包含编码修饰的hG-CSF的基因的表达载体转化的微生物来产生修饰的人粒细胞集落刺激因子(hG-CSF),以产生和分泌经修饰的hG-CSF至周质,所述修饰的hG-CSF 通过将野生型hG-CSF(SEQ ID NO:2)的第1,第2,第3和第17氨基酸中的至少一个替换为其他氨基酸而获得。
摘要:
Disclosed in this invention are an expression vector for the secretive production of human interferon alpha (hIFNα) comprising a polynucleotide encoding a modified E. coli thermostable enterotoxin II signal sequence and a polynucleotide encoding hIFNα ligated to the 3′-end thereof; a microorganism transformed with the expression vector; and a process for secretively producing human interferon by culturing the microorganism, the process being capable of secreting a soluble form of active hIFNα, which does not contain an additional methionine residue at its N-terminal, into the periplasm of an E. coli cell.
摘要:
A protein conjugate having a prolonged in vivo half-life of a physiological activity, comprising i) a physiologically active polypeptide, ii) a non-peptidic polymer, and iii) an immunoglobulin, is useful for the development of a polypeptide drug due to the enhanced in vivo stability and prolonged half-life in blood, while reducing the possibility of inducing an immune response.
摘要:
A protein conjugate having a prolonged in vivo half-life of a physiological activity, comprising i) a physiologically active polypeptide, ii) a non-peptidic polymer, and iii) an immunoglobulin, is useful for the development of a polypeptide drug due to the enhanced in vivo stability and prolonged half-life in blood, while reducing the possibility of inducing an immune response.