Binding Analysis of Ferritin with Heme Using α-Casein and Biotinylated-Hemin: Detection of Heme-Binding Capacity of Dpr Derived from Heme Synthesis-Deficient <i>Streptococcus mutans</i>
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- MIENO Ayako
- Laboratory of Veterinary Biochemistry, School of Veterinary Medicine, Kitasato University, Aomori 034–8628, Japan
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- YAMAMOTO Yuji
- Laboratory of Cellular Microbiology, School of Veterinary Medicine, Kitasato University, Aomori 034–8628, Japan
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- YOSHIKAWA Yasunaga
- Laboratory of Veterinary Biochemistry, School of Veterinary Medicine, Kitasato University, Aomori 034–8628, Japan
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- WATANABE Kiyotaka
- Laboratory of Veterinary Biochemistry, School of Veterinary Medicine, Kitasato University, Aomori 034–8628, Japan
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- MUKAI Takao
- Laboratory of Cellular Microbiology, School of Veterinary Medicine, Kitasato University, Aomori 034–8628, Japan
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- ORINO Koichi
- Laboratory of Veterinary Biochemistry, School of Veterinary Medicine, Kitasato University, Aomori 034–8628, Japan
Bibliographic Information
- Other Title
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- Binding Analysis of Ferritin with Heme Using α-Casein and Biotinylated-Hemin : Detection of Heme-Binding Capacity of Dpr Derived from Heme Synthesis-Deficient Streptococcus mutans
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Abstract
Bacterial and mammalian ferritins are known to bind heme. The use of α-casein and biotinylated hemin could be applicable to detection of protein-bound heme and of proteins with heme-binding capacity, respectively. Although commercial horse spleen ferritin and purified horse spleen ferritin (L:H subunit ratio=4) bound to an α-casein-coated plate, and this binding could be inhibited by hemin, recombinant iron-binding protein (rDpr), derived from heme-deficient Streptococcus mutans and expressed in Escherichia coli, did not bind to an α-casein-coated plate. Both horse spleen ferritins bound to α-casein-immobilized beads. Commercial horse spleen ferritin and rDpr showed direct binding to hemin-agarose beads. After preincubation of commercial horse spleen ferritin or rDpr with biotinylated hemin, they showed indirect binding to avidin-immobilized beads through biotinylated hemin. These results demonstrate that α-casein is useful for detection of heme-binding ferritin and that both hemin-agarose and the combination of biotinylated hemin and avidin-beads are useful for detection of the heme-binding capacity of ferritin. In addition, this study also revealed that Dpr, a decameric iron-binding protein, from heme-deficient cells binds heme.
Journal
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- Journal of Veterinary Medical Science
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Journal of Veterinary Medical Science 75 (8), 1101-1105, 2013
JAPANESE SOCIETY OF VETERINARY SCIENCE
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Details 詳細情報について
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- CRID
- 1390282681408016768
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- NII Article ID
- 130003362183
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- NII Book ID
- AA10796138
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- COI
- 1:STN:280:DC%2BC3srht1ShsQ%3D%3D
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- ISSN
- 13477439
- 09167250
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- NDL BIB ID
- 024852892
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- PubMed
- 23545463
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed