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Yanggu, South Korea

Patent
Cj Healthcare Corporation and Alteogen Inc. | Date: 2013-06-05

The present invention relates to a long-acting human growth hormone NexP-hGH protein and its production method. More specifically, it relates to a specific isoform of long-acting human growth hormone NexP-hGH protein in which human growth hormone is fused with a highly glycosylated alpha-1 antitrypsin mutant whereby long-acting properties in vivo are increased. The present invention also relates to a high-purity purification method for NexP-hGH, which includes the steps of: (a) carrying out anion-exchange resin chromatography on a biological emulsion comprising NexP-hGH in which human growth hormone is fused with an alpha-1 antitrypsin mutant; (b) carrying out hydrophobic resin chromatography on the biological emulsion comprising NexP-hGH, or on the eluate produced in step (a); and (c) carrying out affinity chromatography, entailing packing with a resin to which anti-alpha-1 antitrypsin antibody fragments are attached, on the biological emulsion comprising NexP-hGH and on the eluate produced in step (a) or step (b).


The present invention relates to an antibody in which a motif composed of an amino acid or peptide sequence including one or more cysteine residues is bound to the terminus of a parent antibody, particularly the terminus of the heavy chain of the parent antibody. Also, the present invention relates to a modified antibody-drug conjugate (mADC) comprising a drug bound to the antibody, and a method for producing the antibody or the modified antibody-drug conjugate. The modified antibody-drug conjugate according to the invention can accurately deliver the drug to a target cell due its high specificity to antigen, and thus can increase the therapeutic effect of the drug. Also, it can increase the usability of drugs, particularly anticancer drugs, the use of which is restricted due to their toxicity, despite their high efficacy. Moreover, the invention relates to a composition for treatment of diseases, particularly cancers, which comprise the modified antibody-drug conjugate.


The present invention relates to a fusion protein or peptide, the in vivo half-life of which is increased by maintaining in vivo sustained release, and to a method for increasing in vivo half-life using same. A fusion protein or peptide according to the present invention has excellent in vivo stability by binding a physiologically active protein or physiologically active peptide to an alpha-1 antitrypsin or alpha-1 antitrypsin mutant with one or more amino acids mutated to maintain the in vivo sustained release and to significantly increase the half-life thereof in blood (T1/2) compared to an inherent physiologically active protein or physiologically active peptide. Thus, a fusion protein or peptide according to the present invention can be useful in developing a sustained-release preparation of a protein or peptide drug.


Wang X.,Chungnam National University | Ji S.C.,Chungnam National University | Ji S.C.,Seoul National University | Yun S.H.,Chungnam National University | And 4 more authors.
Journal of Bacteriology | Year: 2014

The gal operon of Escherichia coli has 4 cistrons, galE, galT, galK, and galM. In our previous report (H. J. Lee, H. J. Jeon, S. C. Ji, S. H. Yun, H. M. Lim, J. Mol. Biol. 378:318-327, 2008), we identified 6 different mRNA species, mE1, mE2, mT1, mK1, mK2, and mM1, in the gal operon and mapped these mRNAs. The mRNA map suggests a gradient of gene expression known as natural polarity. In this study, we investigated how the mRNAs are generated to understand the cause of natural polarity. Results indicated that mE1, mT1, mK1, and mM1, whose 3′ ends are located at the end of each cistron, are generated by transcription termination. Since each transcription termination is operating with a certain frequency and those 4 mRNAs have 5= ends at the transcription initiation site(s), these transcription terminations are the basic cause of natural polarity. Transcription terminations at galEgalT and galT-galK junctions, making mE1 and mT1, are Rho dependent. However, the terminations to make mK1 and mM1 are partially Rho dependent. The 5′ ends of mK2 are generated by an endonucleolytic cleavage of a pre-mK2 by RNase P, and the 3′ ends are generated by Rho termination 260 nucleotides before the end of the operon. The 5′ portion of pre-mK2 is likely to become mE2. These results also suggested that galK expression could be regulated through mK2 production independent from natural polarity. © 2014, American Society for Microbiology. Source


The present invention relates to a composition for stabilizing TNF-binding protein exhibiting physiological activity, and more specifically, to a composition for stabilizing protein including basic amino acid and sugar and/or ammonium salt, a pharmaceutical formulation including the same, and a method for stabilizing TNF-binding protein. The formulation including basic amino acid; and sugar and/or ammonium salt according to the present invention effectively inhibits aggregation, denaturation and oxidation of TNF-binding protein used for treating various diseases, for example, an anti-TNF-alpha antibody, such that the protein is capable of being preserved and stored for a long time, which is widely usable and effective in a medical field using TNF-binding protein, for example, an anti-TNF-alpha antibody.

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