| Budget Amount *help |
¥7,800,000 (Direct Cost: ¥7,800,000)
Fiscal Year 1986: ¥300,000 (Direct Cost: ¥300,000)
Fiscal Year 1985: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1984: ¥6,500,000 (Direct Cost: ¥6,500,000)
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| Research Abstract |
Plasma albumin mediated the uptake of bromosulfophthalein into the isolated rat hepatocytes. The binding behabiour of albumin to hepatocytes revealed non-specific interaction between them, suggesting that there is not an "albumin-receptor" on the hepatocytes. The interaction of albumin with the hepatocyte induced structural changes in both albumin and the cell membrane, which were detected by ESR, difference absorption spectra and fluorescence depolarization. Furthermore, albumin is capable of inceeasing the membeane permeability. This was demonstrated in the permeability of liposomes.
The effects of absorption promoters on paracellular and transcellular routes in intestinal membrane were investigated. Promoters enhanced the absorption of water as well as drugs. Ouabain suppressed the drug and water absorption by paracellular promoters such as EDTA, taurocholic acid(TC) and capric acid(C10). The increase in water absorption related to that in absorption site blood flow. For paracellular
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mechanism, C10, C12 and mixed micelles (oleic acid and TC) enlarged the membrane pores in water channel and enavled inulin to permeate through them. For transcellular mechanism, the above promoters interacted with membrane protein and lipid, and caused the membrane perturbation to increase the membrane permeability. Consequently, it was shown that many effective promoters are paracellular ones and also increase the transcellular permeability.
fI-protein, a binding protein for acidic substances, was isolated from the cytosol of rat skeletal muscles by Sephadex G-75 (superfine) gel filtration and chromatofocusing. This protein localizes in the interstitial fluid of the muscle and is contained 2.4 mg/g-tissue, determined by fluorescent antibody technique and radial immunodiffussion method, respectively. Ouchterlony double-immunodiffusion indicated that fI-protein was an immunological identity with each fractionated albumin, which was separated by the same procedure as that of fI-protein, fI-protein is like albumin in binding affinity, physicochemical and immunological characteristics. However, the separation profile differs from that of albumin, suggesting that fI-protein originates in the muscle. Less
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