Preparation From Bovine Colostrum Of A Fraction Rich In Latent Transforming Growth Factor-Beta 2 And Cleared Of Most Allergenic Proteins By One-Step Cibacron Blue Chromatography

A strategy was developed for the preparation of a latent transforming growth factor-beta 2 (latent TGF-beta 2) rich fraction from bovine colostrum. Different conventional chromatography techniques were tested to investigate some physicochemical properties of latent TGF-beta 2 complexes to optimize their recovery. Three latent TGF-beta 2 forms were detected by gel filtration (600, 150-250 and 65-150 kDa). Cation exchange chromatography showed that the pH of latent TGF-beta 2 was above pH 7: hydrophobic interaction chromatography showed that the hydrophobicity of latent TGF-beta 2 was much higher than that of other whey proteins. Affinity chromatography on Cibacron Blue 3G was used to separate latent TGF-beta 2 and immunoglobulin G from the most immunogenic proteins, a-lactalbumin, beta-lactoglobulin and albumin. Optimum conditions were determined: preparation of a fraction 26 times richer in TGF-beta 2 than in serocolostrum was obtained with a good yield (up to 70%) of TGF-beta 2, 80% of which was in the latent form. (c) 2009 Elsevier Ltd. All rights reserved.