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. 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. 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. 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.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. For more information on the batch specific expiration date, please contact technical service. For BSA, core and shell effective pore diffusivities are about 0.25 × 10⁻⁷ and 0.6 × 10⁻⁷ cm²/s, respectively, for Capto Core 400, and about 1.6 × 10⁻⁷ and 2.6 × 10⁻⁷ cm²/s, respectively, for Capto Core 700. Please be aware this product may be shipped 90 days before the expiration date.

462314 ISSN: 0021-9673 Subject: adsorption, bovine serum albumin, chromatography, mass transfer, porosity, surface area, thyroglobulin Abstract: 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. Winters, Giorgio Carta Source: Journal of chromatography 2021 v.1651 pp. 2C and Table 1). 2C and Table 1).The flow-through fractions showed only a non-significant reduction of viral titer (Fig. Protein Adsorption on Core-shell Particles: Comparison of Capto™ Core 400 and 700 Resins Author: Xue Mi, Preston Fuks, Sheng-ching Wang, Michael A. Next, particles and proteins smaller than 700 kDa were removed from the supernatant by size exclusion chromatography with a HiScreen Capto Core 700 column ().Again viral titers and purity were determined (Fig.

Capto core 400