The Experts below are selected from a list of 180 Experts worldwide ranked by ideXlab platform
Ken-ichi Inui - One of the best experts on this subject based on the ideXlab platform.
-
Transport of procainamide via H+/tertiary amine antiport system in rabbit intestinal Brush-Border Membrane
American journal of physiology. Gastrointestinal and liver physiology, 2000Co-Authors: Toshiya Katsura, Hiroshi Mizuuchi, Yukiya Hashimoto, Ken-ichi InuiAbstract:Transport characteristics of procainamide in the Brush-Border Membrane isolated from rabbit small intestine were studied by a rapid-filtration technique. Procainamide uptake by Brush-Border membran...
-
transport of procainamide via h tertiary amine antiport system in rabbit intestinal Brush Border Membrane
American Journal of Physiology-gastrointestinal and Liver Physiology, 2000Co-Authors: Toshiya Katsura, Hiroshi Mizuuchi, Yukiya Hashimoto, Ken-ichi InuiAbstract:Transport characteristics of procainamide in the Brush-Border Membrane isolated from rabbit small intestine were studied by a rapid-filtration technique. Procainamide uptake by Brush-Border membran...
-
bestatin transport in rabbit intestinal Brush Border Membrane vesicles
Biochemical Pharmacology, 1994Co-Authors: Mikihisa Takano, Toshiya Katsura, Ken-ichi Inui, Yoshiko Tomita, Masato Yasuhara, Ryohei HoriAbstract:The effect of papain treatment on bestatin uptake by rabbit intestinal Brush-Border Membrane vesicles (BBMVs) was studied. Papain treatment of BBMVs effectively diminished aminopeptidase activity but not bestatin uptake by a H+/dipeptide cotransporter. Bestatin uptake by BBMVs was composed of two saturable components, and after papain treatment the high-affinity component disappeared while the low-affinity component was retained. These findings suggest that high- and low-affinity components represent bestatin binding to aminopeptidase and the true uptake by the H+/dipeptide cotransporter, respectively.
-
transport of organic cation in renal Brush Border Membrane from rats with renal ischemic injury
Biochimica et Biophysica Acta, 1993Co-Authors: Sayako Maeda, Mikihisa Takano, Ken-ichi Inui, Tomonobu Okano, Kou Ohoka, Ryohei HoriAbstract:Transport of tetraethylammonium, an organic cation, has been studied using renal Brush-Border Membrane vesicles isolated from rats with ischemic and ischemia-reperfusion injury, H+ gradient-dependent uptake of tetraethylammonium slightly, but significantly, decreased in Brush-Border Membrane vesicles from ischemic kidneys. When the kidney was reperfused after ischemia, the extent of the decrease of tetraethylammonium uptake was much greater than that after ischemia alone. The Vmax value of tetraethylammonium uptake by Brush-Border Membrane vesicles from reperfused kidneys was decreased compared with control, without any change in the Km value. The tetraethylammonium uptake by the vesicles from reperfused kidneys was decreased both in the presence and absence of the outward H+ gradient (driving force). Uptake of d-glucose in renal Brush-Border Membrane vesicles was also decreased by ischemia and again, reperfusion caused a further decrease of the uptake. Reperfusion also induced marked changes in the enrichment and recovery of marker enzymes in the isolated Brush-Border Membrane fraction compared with ischemia. These findings suggest that renal ischemic injury altered the transport properties of tetraethylammonium as well as d-glucose, and that reperfusion after ischemia induced further damages on these functions in the Brush-Border Membrane.
Ryohei Hori - One of the best experts on this subject based on the ideXlab platform.
-
Identification of Organic Cation Transporter in Rat Renal Brush-Border Membrane by Photoaffinity Labeling
Biological & pharmaceutical bulletin, 1995Co-Authors: Michio Kimura, Mikihisa Takano, Tomohiro Nabekura, Toshiya Katsura, Ryohei HoriAbstract:As an approach to identification of the organic cation transport system in Brush-Border Membranes, we designed a photoaffinity probe, 1-cyano-2-(4-azido [3, 5-3H] benzoylethyl)-3-[2-[[(5-methyl-4-imidazolyl) methyl] thio] ethyl]-guanidine ([3H] AMC) based on the molecular structure of cimetidine, which is taken up by the organic cation transport system in Brush-Border Membrane vesicles. The effect of nonradioactive 1-cyano-2-(4-azidobenzoylethyl)-3-[2-[[(5-methyl-4-imidazolyl) methyl] thio] ethyl] guanidine (AMC) on tetraethylammonium uptake was investigated in rat renal Brush-Border Membrane vesicles. We examined the photolysis of AMC in which the azido group was converted to an active nitrene group using UV light at a wavelength of 254 nm and established a half-life of 7 s. This half-life duration did not significantly impair Brush-Border Membrane vesicles during the exposure to light for photo-labeling. Photoaffinity labeling of Brush-Border Membrane vesicles from the rat renal cortex with [3H] AMC resulted in the covalent incorporation of radioactivity into Membrane polypeptides ; an apparent 36 kDa polypeptide was predominantly labeled. Photolabeling specificity was shown by a reduction in the labeling of the 36 kDa polypeptide in the presence of organic cations, cimetidine, tetraethylammonium and N-methylnicotinamide whereas the organic anion, furosemide, had no effect on labeling patterns. These data demonstrate that AMC, as well as organic cations, cimetidine, tetraethylammonium and N-methylnicotinamide, interact with a common 36 kDa Membrane polypeptide, which may be the transport system or one of its Brush-Border Membrane components.
-
bestatin transport in rabbit intestinal Brush Border Membrane vesicles
Biochemical Pharmacology, 1994Co-Authors: Mikihisa Takano, Toshiya Katsura, Ken-ichi Inui, Yoshiko Tomita, Masato Yasuhara, Ryohei HoriAbstract:The effect of papain treatment on bestatin uptake by rabbit intestinal Brush-Border Membrane vesicles (BBMVs) was studied. Papain treatment of BBMVs effectively diminished aminopeptidase activity but not bestatin uptake by a H+/dipeptide cotransporter. Bestatin uptake by BBMVs was composed of two saturable components, and after papain treatment the high-affinity component disappeared while the low-affinity component was retained. These findings suggest that high- and low-affinity components represent bestatin binding to aminopeptidase and the true uptake by the H+/dipeptide cotransporter, respectively.
-
transport of organic cation in renal Brush Border Membrane from rats with renal ischemic injury
Biochimica et Biophysica Acta, 1993Co-Authors: Sayako Maeda, Mikihisa Takano, Ken-ichi Inui, Tomonobu Okano, Kou Ohoka, Ryohei HoriAbstract:Transport of tetraethylammonium, an organic cation, has been studied using renal Brush-Border Membrane vesicles isolated from rats with ischemic and ischemia-reperfusion injury, H+ gradient-dependent uptake of tetraethylammonium slightly, but significantly, decreased in Brush-Border Membrane vesicles from ischemic kidneys. When the kidney was reperfused after ischemia, the extent of the decrease of tetraethylammonium uptake was much greater than that after ischemia alone. The Vmax value of tetraethylammonium uptake by Brush-Border Membrane vesicles from reperfused kidneys was decreased compared with control, without any change in the Km value. The tetraethylammonium uptake by the vesicles from reperfused kidneys was decreased both in the presence and absence of the outward H+ gradient (driving force). Uptake of d-glucose in renal Brush-Border Membrane vesicles was also decreased by ischemia and again, reperfusion caused a further decrease of the uptake. Reperfusion also induced marked changes in the enrichment and recovery of marker enzymes in the isolated Brush-Border Membrane fraction compared with ischemia. These findings suggest that renal ischemic injury altered the transport properties of tetraethylammonium as well as d-glucose, and that reperfusion after ischemia induced further damages on these functions in the Brush-Border Membrane.
-
Transport Mechanism of Choline in Rat Renal Brush-Border Membrane
Biological & pharmaceutical bulletin, 1993Co-Authors: Mikihisa Takano, Toshiya Katsura, Yoshiko Tomita, Masato Yasuhara, Ryohei HoriAbstract:The transport mechanism of choline was examined using rat renal Brush-Border Membrane vesicles in comparison with tetraethylammonium transport. The stimulatory effect of an outward H+ gradient on choline uptake was weak compared with that on tetraehylammonium uptake. [14C]Tetraethylammonium uptake was cis-inhibited and trans-stimulated by choline, but the effects were less pronounced than those produced by unlabeled tetraethylammonium. [3H]Choline uptake was trans-stimulated by unlabeled choline, but not by tetraethylammonium. An interior-negative Membrane potential induced marked stimulation of choline uptake against its concentration gradient (overshoot phenomenon), and the uptake was saturable with an apparent Km of 0.77 mM. Various compounds such as hemicholinium-3 inhibited the choline uptake by renal Brush-Border Membrane vesicles, but a sulfhydryl reagent did not. These findings suggest that choline can be actively transported by a carrier-mediated system driven by cell interior-negative Membrane potential in renal Brush-Border Membrane, and this system may play an important role in the tubular reabsorption of choline.
Katsumi Miyazaki - One of the best experts on this subject based on the ideXlab platform.
-
Ionic‐diffusion Potential‐dependent Transport of a New Quinolone, Sparfloxacin, Across Rat Intestinal Brush‐Border Membrane
Journal of Pharmacy and Pharmacology, 1998Co-Authors: Ken Iseki, Kaori Tsuji, Masahiro Takada, Mitsuru Sugawara, Michiya Kobayashi, Takeshi Hirano, Shozo Miyazaki, Katsumi MiyazakiAbstract:The mechanism of uptake of sparfloxacin, a new quinolone, by intestinal Brush-Border Membrane vesicles was investigated to clarify whether there is a common transport process for new quinolones mediated by the diffusion potential across the intestinal Membrane bilayer. Sparfloxacin was taken up pH-dependently by rat intestinal Brush-Border Membrane vesicles, behaviour analogous to that of organic cations including enoxacin and ciprofloxacin. Transient overshooting uptake of this quinolone was observed in the presence of an outward H + gradient. Momentary dissipation of the H + gradient by addition of carbonyl cyanide p-(trifluoromethoxy)phenylhydrazone did not affect the uptake of sparfloxacin, and a marked but incomplete reduction in the H + -sensitive overshooting uptake of sparfloxacin was apparent in the voltage-clamped Brush-Border Membrane vesicles. Furthermore, a valinomycin-induced K + -diffusion potential (interior negative) and an inward Cl - -diffusion potential stimulated the initial uptake of sparfloxacin at pH 5.5. Sparfloxacin uptake was inhibited by tetracaine and imipramine. The inhibitory effect of these cations correlated well with changes in Membrane surface charges induced by the presence of tetracaine or imipramine. These results indicate that sparfloxacin transport across the Brush-Border Membrane depends upon the inside-negative ionic diffusion potential, that the H + - or K + -diffusion-potential-dependent uptake of sparfloxacin by intestinal Brush-Border Membrane vesicles is affected by the Membrane surface potential and that inhibition of sparfloxacin uptake originates from changes in the Membrane surface potential caused by the organic cations.
-
Uptake of methylchlorpromazine by Brush-Border Membrane vesicles from rat small intestine.
Biological & pharmaceutical bulletin, 1997Co-Authors: Hiroshi Saitoh, Katsumi MiyazakiAbstract:The uptake of methylchlorpromazine (MCP), a quaternary derivative of chlorpromazine, was investigated using Brush-Border Membrane vesicles islated from rat small intestine. MCP was taken up rapidly by the vesicles, a major part of the uptake being due to binding to the Membrane. Saturable MCP binding to the Brush-Border Membrane was inhibited strongly by chlorpromazine, moderately by propantheline and imipramine, and slightly but significantly by methylbenactyzine and mepenzolate. However, choline and tetramethylammonium failed to exhibit any such inhibitory effect. The movement of MCP into the intravesicular space was driven by an inside-negative transMembrane electrical potential difference (TEPD) induced by NaSCN or valinomycin. There was no effect of TEPD on MCP binding to the Brush-Border Membrane. The data suggested that both rapid binding to the Brush-Border Membrane and inside-negative TEPD, which is present physiologically across the Membrane, play a significant role in the absorptive movements of MCP across intestinal epithelium.
-
Uptake of 6‐Mercaptopurine Riboside via the Nucleoside Transporter in the Human Intestinal Brush‐Border Membrane
Pharmacy and Pharmacology Communications, 1995Co-Authors: Ken Iseki, Mitsuru Sugawara, Michiya Kobayashi, Imad Naasani, Toshie Fujiwara, Katsumi MiyazakiAbstract:The transport systems of 6-mercaptopurine riboside (6-MPR), a nucleoside analogue, in the human jejunal Brush-Border Membrane and in the human epithelial cell line, Caco-2, were investigated. The transport activities of 6-MPR were found to be dependent upon an inward Na+-gradient at pH 5·5. Trans-stimulation studies indicated that the uptakes of both [3H]adenosine and [3H]uridine were significantly increased by the presence of 6-MPR inside the human Brush-Border Membrane vesicles. The uptake of 6-MPR from the apical side of Caco-2 monolayer was sensitive for an inward-directed Na+-gradient, and a greater uptake was observed at an acidic medium (pH 5·5>7·5). Moreover, both adenosine and uridine were significantly effective in inhibiting the 6-MPR uptake by Caco-2. These results indicate that an analogue of adenosine, 6-MPR, is able to be taken up via the Na+-gradient-dependent purine- and pyrimidine-nucleosides transport systems in the human intestinal Brush-Border Membrane.
-
uptake of 6 mercaptopurine riboside via the nucleoside transporter in the human intestinal Brush Border Membrane
Pharmacy and Pharmacology Communications, 1995Co-Authors: Ken Iseki, Mitsuru Sugawara, Michiya Kobayashi, Imad Naasani, Toshie Fujiwara, Katsumi MiyazakiAbstract:The transport systems of 6-mercaptopurine riboside (6-MPR), a nucleoside analogue, in the human jejunal Brush-Border Membrane and in the human epithelial cell line, Caco-2, were investigated. The transport activities of 6-MPR were found to be dependent upon an inward Na+-gradient at pH 5·5. Trans-stimulation studies indicated that the uptakes of both [3H]adenosine and [3H]uridine were significantly increased by the presence of 6-MPR inside the human Brush-Border Membrane vesicles. The uptake of 6-MPR from the apical side of Caco-2 monolayer was sensitive for an inward-directed Na+-gradient, and a greater uptake was observed at an acidic medium (pH 5·5>7·5). Moreover, both adenosine and uridine were significantly effective in inhibiting the 6-MPR uptake by Caco-2. These results indicate that an analogue of adenosine, 6-MPR, is able to be taken up via the Na+-gradient-dependent purine- and pyrimidine-nucleosides transport systems in the human intestinal Brush-Border Membrane.
-
transport characteristics of cephalosporin antibiotics across intestinal Brush Border Membrane in man rat and rabbit
Journal of Pharmacy and Pharmacology, 1992Co-Authors: Mitsuru Sugawara, Katsumi Miyazaki, Ken Iseki, Takaki Toda, Hiroshi Shiroto, Yukifumi Kondo, Junichi UchinoAbstract:The uptake of orally active cephalosporins, ceftibuten and cephradine, by intestinal Brush-Border Membrane vesicles isolated from man, rat and rabbit was studied. In the presence of an inward H+ gradient, ceftibuten but not cephradine was taken up into intestinal Brush-Border Membrane vesicles of man and rat against the concentration gradient (overshoot phenomenon). In rabbit jejunal Brush-Border Membrane vesicles, the uptake of both cephalosporins in the presence of an inward H+ gradient exhibited the overshoot phenomenon. In human and rat vesicles, the initial uptake of ceftibuten was strongly inhibited by compound V, an analogue of ceftibuten, but the uptake of cephradine was not affected by any of the cephalosporins tested, whereas in the rabbit Brush-Border Membrane vesicles, initial uptake of both ceftibuten and cephradine were markedly inhibited by all cephalosporins and dipeptides used. These results suggest that the transport characteristics of human and rat intestinal Brush-Border Membrane for cephalosporins are comparable, and that rabbit is an inadequate animal for investigating the transport characteristics of beta-lactam antibiotics.
Toshiya Katsura - One of the best experts on this subject based on the ideXlab platform.
-
Transport of procainamide via H+/tertiary amine antiport system in rabbit intestinal Brush-Border Membrane
American journal of physiology. Gastrointestinal and liver physiology, 2000Co-Authors: Toshiya Katsura, Hiroshi Mizuuchi, Yukiya Hashimoto, Ken-ichi InuiAbstract:Transport characteristics of procainamide in the Brush-Border Membrane isolated from rabbit small intestine were studied by a rapid-filtration technique. Procainamide uptake by Brush-Border membran...
-
transport of procainamide via h tertiary amine antiport system in rabbit intestinal Brush Border Membrane
American Journal of Physiology-gastrointestinal and Liver Physiology, 2000Co-Authors: Toshiya Katsura, Hiroshi Mizuuchi, Yukiya Hashimoto, Ken-ichi InuiAbstract:Transport characteristics of procainamide in the Brush-Border Membrane isolated from rabbit small intestine were studied by a rapid-filtration technique. Procainamide uptake by Brush-Border membran...
-
Identification of Organic Cation Transporter in Rat Renal Brush-Border Membrane by Photoaffinity Labeling
Biological & pharmaceutical bulletin, 1995Co-Authors: Michio Kimura, Mikihisa Takano, Tomohiro Nabekura, Toshiya Katsura, Ryohei HoriAbstract:As an approach to identification of the organic cation transport system in Brush-Border Membranes, we designed a photoaffinity probe, 1-cyano-2-(4-azido [3, 5-3H] benzoylethyl)-3-[2-[[(5-methyl-4-imidazolyl) methyl] thio] ethyl]-guanidine ([3H] AMC) based on the molecular structure of cimetidine, which is taken up by the organic cation transport system in Brush-Border Membrane vesicles. The effect of nonradioactive 1-cyano-2-(4-azidobenzoylethyl)-3-[2-[[(5-methyl-4-imidazolyl) methyl] thio] ethyl] guanidine (AMC) on tetraethylammonium uptake was investigated in rat renal Brush-Border Membrane vesicles. We examined the photolysis of AMC in which the azido group was converted to an active nitrene group using UV light at a wavelength of 254 nm and established a half-life of 7 s. This half-life duration did not significantly impair Brush-Border Membrane vesicles during the exposure to light for photo-labeling. Photoaffinity labeling of Brush-Border Membrane vesicles from the rat renal cortex with [3H] AMC resulted in the covalent incorporation of radioactivity into Membrane polypeptides ; an apparent 36 kDa polypeptide was predominantly labeled. Photolabeling specificity was shown by a reduction in the labeling of the 36 kDa polypeptide in the presence of organic cations, cimetidine, tetraethylammonium and N-methylnicotinamide whereas the organic anion, furosemide, had no effect on labeling patterns. These data demonstrate that AMC, as well as organic cations, cimetidine, tetraethylammonium and N-methylnicotinamide, interact with a common 36 kDa Membrane polypeptide, which may be the transport system or one of its Brush-Border Membrane components.
-
bestatin transport in rabbit intestinal Brush Border Membrane vesicles
Biochemical Pharmacology, 1994Co-Authors: Mikihisa Takano, Toshiya Katsura, Ken-ichi Inui, Yoshiko Tomita, Masato Yasuhara, Ryohei HoriAbstract:The effect of papain treatment on bestatin uptake by rabbit intestinal Brush-Border Membrane vesicles (BBMVs) was studied. Papain treatment of BBMVs effectively diminished aminopeptidase activity but not bestatin uptake by a H+/dipeptide cotransporter. Bestatin uptake by BBMVs was composed of two saturable components, and after papain treatment the high-affinity component disappeared while the low-affinity component was retained. These findings suggest that high- and low-affinity components represent bestatin binding to aminopeptidase and the true uptake by the H+/dipeptide cotransporter, respectively.
-
Transport Mechanism of Choline in Rat Renal Brush-Border Membrane
Biological & pharmaceutical bulletin, 1993Co-Authors: Mikihisa Takano, Toshiya Katsura, Yoshiko Tomita, Masato Yasuhara, Ryohei HoriAbstract:The transport mechanism of choline was examined using rat renal Brush-Border Membrane vesicles in comparison with tetraethylammonium transport. The stimulatory effect of an outward H+ gradient on choline uptake was weak compared with that on tetraehylammonium uptake. [14C]Tetraethylammonium uptake was cis-inhibited and trans-stimulated by choline, but the effects were less pronounced than those produced by unlabeled tetraethylammonium. [3H]Choline uptake was trans-stimulated by unlabeled choline, but not by tetraethylammonium. An interior-negative Membrane potential induced marked stimulation of choline uptake against its concentration gradient (overshoot phenomenon), and the uptake was saturable with an apparent Km of 0.77 mM. Various compounds such as hemicholinium-3 inhibited the choline uptake by renal Brush-Border Membrane vesicles, but a sulfhydryl reagent did not. These findings suggest that choline can be actively transported by a carrier-mediated system driven by cell interior-negative Membrane potential in renal Brush-Border Membrane, and this system may play an important role in the tubular reabsorption of choline.
Helmut Hauser - One of the best experts on this subject based on the ideXlab platform.
-
The uptake of cholesterol at the small‐intestinal Brush Border Membrane is inhibited by apolipoproteins
FEBS letters, 1997Co-Authors: Dario Boffelli, Georg Schulthess, Sabina Compassi, Franz E Weber, Moritz Werder, Michael C. Phillips, Helmut HauserAbstract:Abstract The uptake of free and esterified cholesterol at the Brush Border Membrane is protein-mediated. Here we show that this sterol uptake is effectively inhibited by exchangeable serum apolipoproteins. Binding of the apolipoprotein to the Brush Border Membrane mediates the inhibitory effect. Evidence is presented to show that the structural motif responsible for the inhibition is the amphipathic α-helix.
-
A comparative study of sterol absorption in different small-intestinal Brush Border Membrane models.
Journal of lipid research, 1996Co-Authors: Georg Schulthess, Sabina Compassi, Dario Boffelli, Franz E Weber, Moritz Werder, Helmut HauserAbstract:We reported previously that the absorption of cholesterol and long-chain cholesteryl esters by rabbit small-intestinal Brush Border Membranes (BBMV) is protein-mediated (Thurnhofer, H., and H. Hauser. 1990. Biochemistry. 29:2142-2148; Compassi, S., M. Werder, D. Boffelli, F. E. Weber, H. Hauser, and G. Schulthess. 1995. Biochemistry. 34: 16473-16482). Evidence is presented for similar cholesterol transport activities in rabbit, pig, and human BBMV. As BBMV are subject to a number of limitations and the influence of these on sterol absorption is unknown, it is desirable to verify results obtained with this model system in other Brush Border Membrane models more closely related to the in vivo situation. Sterol absorption in intact enterocytes parallels the absorption measured in BBMV, provided that both model systems are normalized to equal sucrase activity. The parallel behavior of the two Brush Border Membrane models lends support to our previous conclusion that the Brush Border Membrane takes up free and esterified cholesterol in a facilitated and energy-independent process. The absorption of sterols in small-intestinal segments mounted in the Ussing chamber is shown to be a complex process in which the diffusion of the bile salt micelles to the Brush Border Membrane is rate-limiting. All Brush Border Membrane models share the disadvantage of being unstable and subject to degradation. The seriousness of the problem increases apparently with the complexity of the model, i.e., in the order BBMV-->enterocytes-->intestinal segments. One main conclusion of this study is that no Brush Border Membrane model is sufficient and satisfactory, therefore conclusive work in lipid absorption can never be based on a single Brush Border Membrane model.
-
absorption of monoacylglycerols by small intestinal Brush Border Membrane
Biochemistry, 1994Co-Authors: Georg Schulthess, Sabina Compassi, Dario Boffelli, Franz E Weber, G Lipka, Fritz Paltauf, Helmut HauserAbstract:The absorption of monoacylglycerol by small intestinal Brush Border Membrane is a passive process, i.e., the movement of monoacylglycerol from small unilamellar phospholipid vesicles as donor particles through the aqueous medium and the incorporation into the outer monolayer of the lipid bilayer of the Brush Border Membrane are passive processes involving diffusion of the lipid along a concentration gradient. Small unilamellar vesicles of egg phosphatidylcholine containing 1 mol 7% of radiolabeled hexadecylglycerol were used as donor, and rabbit small intestinal Brush Border Membrane vesicles or intact enterocytes isolated from pig jejunum, as acceptor. Hexadecylglycerol was employed as a lipase-resistant model compound for monoacylglycerols. Both acceptor Membranes behave similarly in terms of hexadecylglycerol absorption: the kinetics of hexadecylglycerol absorption are biphasic. The initial fast phase is due to the movement of hexadecylglycerol from the donor particle through the aqueous medium to the outer lipid monolayer of the acceptor Membrane, and the second slow phase probably involves the flip-flop motion of hexadecylglycerol from the outer to the inner monolayer of the acceptor Membrane. The values for the pseudo-first-order rate constants of the initial fast phase for hexadecylglycerol absorption are relatively large and primarily determined by the high solubility (cmc) of hexadecylglycerol in aqueous media. The pseudo-first-order rate constants depend linearly on the protein (lipid) concentration of the acceptor Membrane, indicating that the on rate of the hexadecylglycerol into the Brush Border Membrane is rate limiting. The mechanism of the hexadecylglycerol absorption involves mainly monomer diffusion and probably collision-induced transfer.
