Abstract
A strategy was developed for the preparation of a latent transforming growth factor-β2 (latent TGF-β2) rich fraction from bovine colostrum. Different conventional chromatography techniques were tested to investigate some physicochemical properties of latent TGF-β2 complexes to optimize their recovery. Three latent TGF-β2 forms were detected by gel filtration (600, 150–250 and 65–150 kDa). Cation exchange chromatography showed that the p I of latent TGF-β2 was above pH 7; hydrophobic interaction chromatography showed that the hydrophobicity of latent TGF-β2 was much higher than that of other whey proteins. Affinity chromatography on Cibacron Blue 3G was used to separate latent TGF-β2 and immunoglobulin G from the most immunogenic proteins, α-lactalbumin, β-lactoglobulin and albumin. Optimum conditions were determined: preparation of a fraction 26 times richer in TGF-β2 than in serocolostrum was obtained with a good yield (up to 70%) of TGF-β2, 80% of which was in the latent form.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
