The effect of different folate forms on denaturation of bovine folate binding protein |
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| Authors: | Linnéa Nygren-Babol Karin Landström Karonen |
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| Affiliation: | 1. Department of Pathology and Immunology, Washington University School of Medicine in St Louis, St Louis, MO 63110, USA;2. Department of Chemistry, Box 1134, Washington University, One Brookings Drive, St. Louis, Mo, 63130, USA;3. Center for Microbial Pathogenesis, Institute for Biomedical Sciences, Georgia State University, Atlanta, GA 30303, USA;4. Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA |
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| Abstract: | Denaturation temperatures (Tmax) of folate binding protein (FBP) complexed with various folate derivatives were studied using differential scanning calorimetry. Surface plasmon resonance technique was used to elucidate the effect of heat treatment, i.e., pasteurization and UHT treatment, of FBP on FBP content and its binding capacity to folate. The folate derivatives studied were (6S)5-HCO-H4folate, (6S)5-CH3-H4folate and pteroyl-l-glutamic acid (PteGlu). The results showed that different folate forms affected the heat denaturation temperature of FBP differently. Apo-FBP underwent an endothermic transition with a maximum at 60.5 ± 0 °C. After ligand binding, the maximum of the denaturation shifted with a transition maximum at 72.4 ± 0.3 °C for (6S)5-HCO-H4folate and 78.7 ± 0.5 °C for (6S)5-CH3-H4folate. The highest temperature shift was observed for PteGlu with maximum transition temperature at 83.7 ± 0.2 °C. Pasteurization temperatures did not eliminate the binding capacity of FBP regardless of folate form bound, whereas the UHT-treatment did. |
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