1993 Fiscal Year Final Research Report Summary
化学伝達物質としてのウシラクトフェリンの機能とその構造ユニットの解明
| Project/Area Number |
03660289
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
畜産化学
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| Research Institution | Obihiro University of Agriculture and Veterinary Medicine |
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Principal Investigator |
SHIMAZAKI Kei-ichi OBIHIRO UNIV.OF AGR.& VET.MED.DEPT.OF BIORESOURCE CHEM.ASSOCIATE PROFESSOR, 畜産学部, 助教授 (10091547)
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| Project Period (FY) |
1991 – 1993
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| Keywords | lactoferrin / milk protein / monocyte / Trypanosoma / fragments |
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| Research Abstract |
The C terminal half molecule (C lobe) of bovine lactoferrin was isolated by mild tryptic hydrolysis of lactoferrin followed by gel filtration and ion-exchange chromatography. The idntity of the fragment was established by determining its N terminal and C terminal amino acid sequences and comparing them with the amino acid sequence of intact lactoferrin.
The binding properties of intact lactoferrin and its fragments have been tested with bovine monocyte and with Trypanosoma cruzi. The specific binding with bovine lactoferrin was studied. Lactoferrin isolated from mature bovine milk by chromatographic method was used and labeled by ^<125>I-Bolton-Hunter reagent. From the binding assay, it was found that bovine milk lactoferrin could bind to bovine monocyte, specifically. And intact lactoferrin showed the binding ability to Trypanosoma cruzi (amastigote form). However, C terminal half molecule of bovine lactoferrin loses the binding capacity against Trypanosoma cruzi. Amastigote of Trypanosoma cruzi was obtained from mouse embryo fibroblast culture. The binding was studied by the method of the direct immunofluorescence test using FITC-labeled anti-bovine lactoferrin antibody (rabbit).
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