C12Y304/00- Hydrolases acting on peptide bonds, i.e.C07K1/20- Partition-, reverse-phase or hydrophobic interaction chromatography. C07K1/16- Extraction Separation Purification by chromatography.C07K1/14- Extraction Separation Purification.processes for the organic chemical preparation of peptides or proteins of any length C07K1/00- General methods for the preparation of peptides, i.e.chromatography characterised by the separation mechanism involving ionic interaction B01D15/327- Reversed phase with hydrophobic interaction.chromatography characterised by the separation mechanism B01D15/00- Separating processes involving the treatment of liquids with solid sorbents Apparatus therefor.B01- PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL.Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea C12N9/48- Hydrolases (3) acting on peptide bonds (3.4).C12N9/00- Enzymes Proenzymes Compositions thereof Processes for preparing, activating, inhibiting, separating or purifying enzymes.C12N- MICROORGANISMS OR ENZYMES COMPOSITIONS THEREOF PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS MUTATION OR GENETIC ENGINEERING CULTURE MEDIA.C12- BIOCHEMISTRY BEER SPIRITS WINE VINEGAR MICROBIOLOGY ENZYMOLOGY MUTATION OR GENETIC ENGINEERING.C07K14/33- Peptides having more than 20 amino acids Gastrins Somatostatins Melanotropins Derivatives thereof from bacteria from Clostridium (G).C07K14/195- Peptides having more than 20 amino acids Gastrins Somatostatins Melanotropins Derivatives thereof from bacteria.C07K14/00- Peptides having more than 20 amino acids Gastrins Somatostatins Melanotropins Derivatives thereof.Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.) Filing date Publication date Application filed by (주)제테마 filed Critical (주)제테마 Publication of KR20200121246A publication Critical patent/KR20200121246A/en Application granted granted Critical Publication of KR102447441B1 publication Critical patent/KR102447441B1/en Links ( en Inventor 김재영 남정선 김승호 최승관 임현택 최진희 Original Assignee (주)제테마 Priority date (The priority date is an assumption and is not a legal conclusion. Google Patents KR20200121246A - A Purification Method of Botulinum Toxin Published by Elsevier B.V.KR20200121246A - A Purification Method of Botulinum Toxin However, some of this advantage is lost if the feed is a mixture of BSA and Tg since, in this case, Tg binding leads to greater diffusional hindrance for BSA.Ĭore-shell resins Diffusional hindrance Dynamic binding capacity Flow-through purification Modeling.Ĭopyright © 2021. Column measurements show that, despite the higher static capacity of Capto Core 400 for BSA, the dynamic binding capacity is greater for Capto Core 700 as a result of its faster kinetics. Adsorbed Tg further hinders diffusion of BSA in both resins. These values decrease dramatically for Tg to 0.022 × 10 -7 and 0.088 × 10 -7 cm 2/s and to 0.13 × 10 -7 and 0.59 × 10 -7 cm 2/s for Capto Core 400 and 700, respectively. For BSA, core and shell effective pore diffusivities are about 0.25 × 10 -7 and 0.6 × 10 -7 cm 2/s, respectively, for Capto Core 400, and about 1.6 × 10 -7 and 2.6 × 10 -7 cm 2/s, respectively, for Capto Core 700. Mass transfer in both resins is affected by diffusional resistances through the shell and within the adsorbing core. However, for the much larger Tg, the attainable capacity is substantially larger for Capto Core 700. Because of the smaller pores and higher surface area, the BSA binding capacity of Capto Core 400 is approximately double that of Capto Core 700. Although shell thicknesses are comparable (3.6 and 4.2 µm for Capto Core 400 and 700, respectively), the two resins differ substantially in pore size (pore radii of 19 and 50 nm, respectively). Both resins are agarose-based and contain an adsorbing core surrounded by an inert shell. Structural and functional characteristics of the two core-shell resins Capto™ Core 400 and 700, which are useful for the flow-through purification of bioparticles such as viruses, viral vectors, and vaccines, are compared using bovine serum albumin (BSA) and thyroglobulin (Tg) as models for small and large protein contaminants.
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