Intra-intestinal kinetics and absorption mechanism of digestion-resisitant maclomolecular food components
Project/Area Number |
14360073
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
食品科学・栄養科学
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Research Institution | Nagoya University |
Principal Investigator |
MATSUDA Tsukasa Nagoya University, Graduate School of Bioagricultueral Sciences, Associate Professor, 大学院・生命農学研究科, 教授 (20144131)
|
Co-Investigator(Kenkyū-buntansha) |
NADANO Daita Nagoya University, Graduate School of Bioagricultueral Sciences, Associate Professor, 大学院・生命農学研究科, 助教授 (00228074)
AOKI Naohito Mie Univrsily, Faculty of Bioresources Science, Associate Professor, 生物資源学部, 助教授 (40242846)
SATO Chihiro Nagoya University, Bioscience and Biotechnology Center, Associate Professor, 生物機能開発利用研究センター, 助教授 (10343211)
|
Project Period (FY) |
2002 – 2004
|
Project Status |
Completed (Fiscal Year 2004)
|
Budget Amount *help |
¥14,900,000 (Direct Cost: ¥14,900,000)
Fiscal Year 2004: ¥2,300,000 (Direct Cost: ¥2,300,000)
Fiscal Year 2003: ¥4,400,000 (Direct Cost: ¥4,400,000)
Fiscal Year 2002: ¥8,200,000 (Direct Cost: ¥8,200,000)
|
Keywords | digestibility-resistant / intestinal absorption / kinetics in blood / egg albumin / glycoprotein / ELISA / オボアルブミン / トリプシンインヒビター |
Research Abstract |
Egg albumin (ovalbumin:OVA) is resistant to proteolytic hydrolysis and known to be a major allergenic protein in egg allergy. By using egg albumin as a model macromoleculer food component, the absorption of OVA from mouse intestinal tract into body and the kinetics of OVA in circulating peripheral blood were investigated. After oral administration of OVA (10 mg) to mice, peripheral blood was collected and then serum was separated from coagulated blood. The OVA concentration in the serum was determined to be 10-50 ng/ml by EUSA, and the OVA in the serum was concentrated by immuno-affinity precipitation using anti-OVA antibodies coupled to Sepharose. In SDS-PAGE analysis, the OVA recovered from peripheral blood revealed a single major protein band with a molecular mass identical to intact OVA and a minor band with a slightly smaller molecular mass. No band corresponding to OVA fragments with smaller molecular masses, which had been demonstrated to be the major components of OVA antigens in the mouse small intestine. Furthermore, two-dimensional gel electrophoresis demonstrated that the OVA recovered from blood was composed of 4-6 protein spots with different pI but with the same molecular mass, and that the basic protein spots were dominant as compared with those of intacl OVA, suggesting that the pI of OVA was shifted to more basic ones during the intestinal absorption or the migration in circulating blood. Such a pI shift was not observed for OVA incubated in vitro with mouse serum. Taken together, it is suggested that a small portion of orally administered OVA could escape from intestinal proteolytic digestion and be absorbed as an intact form, but with a slight modification, across intestinal epithelium into the blood stream. Thus, it might be possible that orally administered bio-active proteins exert its biological function in peripheral tissues and organs.
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Report
(4 results)
Research Products
(14 results)