Cross-Linking of Egg White Riboflavin-Binding Protein by Calcium Phosphate
| Autor: | Y. Yamao, Y. Kumasaki, Y. Kako, T. Aoki, E. Yonemasu |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Calcium Phosphates
Dimer Biophysics chemistry.chemical_element Riboflavin Calcium Biochemistry Dephosphorylation Gel permeation chromatography chemistry.chemical_compound Egg White Glyceraldehyde Animals Molecular Biology Chromatography High Pressure Liquid Chromatography Calcium-Binding Proteins Egg Proteins Membrane Transport Proteins Phosphate Cross-Linking Reagents chemistry Carrier Proteins Chickens Egg white |
| Zdroj: | Archives of Biochemistry and Biophysics. 305:242-246 |
| ISSN: | 0003-9861 |
| Popis: | No larger molecular weight component appeared in the high-performance gel chromatogram when calcium alone was added to the riboflavin-binding protein solution (RfBP), indicating that calcium alone did not aggregate it. RfBP bound calcium, but the amount of bound calcium decreased markedly upon dephosphorylation. Cross-linked RfBP, which was detected by high-performance gel chromatography using simulated milk ultrafiltrate as the effluent, was formed when calcium and phosphate were added. Cross-linking of RfBP was confirmed by ultracentrifugal analysis. RfBP was found to be cross-linked through its phosphate groups, since no cross-linked fraction was detected when calcium and phosphate were added to a dephosphorylated RFBP solution. RfBP cross-linked by calcium phosphate formed at 12-20 mM calcium, 13-17 mM phosphate, and 10 mM citrate was a dimer, since its retention time was consistent with that of the dimer cross-linked by glyceraldehyde. The physiological function of phosphate groups of RfBP was also discussed. |
| Databáze: | OpenAIRE |
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