Binding of human serum proteins to titanium dioxide particles in vitro
| Autor: | Mazen S. K. Zaqout, Toshihiko Myojo, Hideki Igisu, Tomoyuki Sumizawa, Toshiaki Higashi |
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| Rok vydání: | 2011 |
| Předmět: |
Adult
Male Globulin Plasma protein binding In Vitro Techniques medicine Humans Coloring Agents Polyacrylamide gel electrophoresis Serum Albumin Gel electrophoresis Titanium Chromatography biology Chemistry Public Health Environmental and Occupational Health Albumin Middle Aged Human serum albumin Blood proteins Electrophoresis Immunology biology.protein Electrophoresis Polyacrylamide Gel gamma-Globulins medicine.drug Protein Binding |
| Zdroj: | Journal of occupational health. 53(2) |
| ISSN: | 1348-9585 |
| Popis: | Objectives: To determine the capacity of human serum proteins to bind to titanium dioxide (TiO2) particles of different polymorphs and sizes. Methods: TiO2 particles were mixed with diluted human serum, purified human serum albumin (HSA) or purified human serum gamma-globulin (HGG) solutions. After incubation at 37°C for 1 h, the particles were sedimented by centrifugation, and proteins in the supernatant, as well as those bound to the particles, were analyzed. Results: The total protein concentration in the supernatant was lowered by TiO2, whereas the albumin/globulin ratio was elevated by the particles. Incubation with TiO2 also lowered the immunoglobulin, pre-albumin, beta2-microglobulin, ceruloplasmin and retinol-binding protein levels, but not ferritin levels, in the supernatant. After sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), proteins in the supernatant, especially HGG, were observed to decrease, while those released from the particles (after adding 1% SDS and heating) increased, depending on the dose of TiO2. Purified HGG and HSA were also bound to TiO2, although the former appeared to have a higher affinity. All the proteins tested showed the highest binding potency to the amorphous particles ( |
| Databáze: | OpenAIRE |
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