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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Agriculture / Faculty of Agriculture >
Peer-reviewed Journal Articles, etc >
Characterization of Binding Between the Rat Small Intestinal Brush-border Membrane and Dietary Proteins in the Sensory Mechanism of Luminal Dietary Proteins.
| Title: | Characterization of Binding Between the Rat Small Intestinal Brush-border Membrane and Dietary Proteins in the Sensory Mechanism of Luminal Dietary Proteins. |
| Authors: | Hira, Tohru Browse this author | | Hara, Hiroshi Browse this author →KAKEN DB | | Tomita, Fusao Browse this author |
| Keywords: | dietary protein | | brush-border membrane | | casein | | binding |
| Issue Date: | May-2001 |
| Publisher: | Japan Society for Bioscience, Biotechnology, and Agrochemistry |
| Journal Title: | Bioscience Biotechnology and Biochemistry |
| Volume: | 65 |
| Issue: | 5 |
| Start Page: | 1007 |
| End Page: | 1015 |
| Publisher DOI: | 10.1271/bbb.65.1007 |
| PMID: | 11440110 |
| Abstract: | Dietary proteins are recognized by the gastrointestinal tract to display physiological functions, however, the sensory mechanism of the intestinal mucosa is not known. We examined binding properties between the rat small intestinal brush-border membrane (BBM) and proteins by using a surface plasmon resonance biosensor. BBM and solubilized BBM prepared from the rat jejunum bound to casein immobilized on the sensor surface, but not to bovine serum albumin. The ileal BBM showed less binding to casein than the jejunal BBM. Solubilized BBM binding to immobilized α-casein was slightly inhibited by aminopeptidase inhibitors, but still more inhibited by addition of casein with the inhibitors. Guanidinated casein inhibited the solubilized BBM binding to α-casein more strongly than casein (casein sodium and α-casein) inhibited. Trypsinization of solubilized BBM abolished its binding activity to α-casein. These results indicate that some membrane protein, but not aminopeptidases, contained in BBM interacts with dietary proteins, and that guanidinated casein has a higher affinity for BBM than intact casein. These binding intensities for proteins were closely correlated to physiological responsiveness, and are possibly involved in a sensory system for dietary protein in the intestine. |
| Relation: | http://www.jstage.jst.go.jp/ |
| Type: | article |
| URI: | http://hdl.handle.net/2115/15861 |
| Appears in Collections: | 農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 原 博
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