Thesis (Ph.D) - University of Birmingham, Dept of Medicine.
|Statement||by Gillian Grafton.|
Kinetics of myo-inositol (MI) uptake into primary cultures of bovine corneal endothelial cells (CEC) were studied. Confluent corneal endothelial cells accumulated 3H-MI in a time dependent and saturable process. At a narrow range of external concentrations of 3H-MI ( microM), the Na(+)-dependent MI uptake followed saturation by: 4. Finally, the myo-inositol transport is trans-activated by myo-inositol itself, but not by D-glucose. it is concluded that myo-inositol is transported into rat intesti:te BBMV by a specific transport system, which is also able to bind D-glucose, but not efficiently transport it across the by: The transport obeyed saturation kinetics with an apparent Km for myo-inositol of mM, myo-Inositol analogs, such as scyllo-inositol, 2-inosose, mannitol, and 1,2-cyclohexanediol, had no effect on myo-inositol uptake, myo-Inositol uptake required metabolic energy. Removal of D-glucose resulted in a loss of activity, Cited by: The kinetics of the sodium-dependent system fitted a ‘velocity type’ co-transport model where binding of sodium ion to the carrier increased the velocity (V max 28 to pmol myo-inositol/μm DNA per 20 min when [Na +] varied from 9 to mM) but not the affinity for myo-inositol (K m to mM when [Na +] varied from 9 to mM).Cited by:
Candida myo-inositol transport was sodium-independent but proton-coupled with an apparent K(m) value of +/- nM for H(+), equal pH +/- , suggesting that the C. albicans myo. Myo-Inositol transport by Salmonella enterica serovar Typhimurium Article (PDF Available) in Microbiology (Pt 1) October with 43 Reads How we measure 'reads'. Myo -inositol attachment induces a reorientation of the transporter, thereby closing the extracellular gate. The intracellular gate is opened during the third state and the substrates are released into the cell. The next two states are defined by closing the intracellular gate and opening the extracellular gate, Cited by: Sodium/myo-inositol cotransporter is a protein that in humans is encoded by the SLC5A3 gene. Expression of the myo-inositol transport protein is regulated by osmotic s: SLC5A3, BCW2, SMIT, SMIT1, SMIT2, .
TRANSPORT OF wyo-INOSITOL IN CHICKEN RETICULOCYTES ^•TOZO5S Myo-inositol mM) FIG. 2. The rate of uptake of wiyo-inositol by reticulocytes (solid line) and mature cells (dashed line) versus concentration ( mM) of wyo-inositol in the basic by: 7. The unidirectional transport of [3H]myo-inositol across cerebral capillaries, the anatomical locus of the blood-brain barrier, was measured using an in situ rat brain perfusion technique. Myo-inositol was transported across the blood-brain barrier by a low capacity, saturable system with a one-half saturation concentration of ∼ mM. The permeability surface-area product was ×10−5S Cited by: Kinetics of Myo‐inositol transport in rat ocular lens Kinetics of Myo‐inositol transport in rat ocular lens Diecke, F. P. J.; Beyer‐Mears, A.; Mistry, K. Literature Cited Alvarado, F., and Crane, R. K. () Phlorizin as competitive inhibitor of the active transport of sugars by hamster small intestine in vitro. Three different mammalian myo-inositol cotransporters are currently known; two are the Na +-coupled SMIT1 and SMIT2 tabulated below and the third is proton-coupled HMIT (SLC2A13).SMIT1 and SMIT2 have a widespread and overlapping tissue location but in polarized cells, such as the Madin-Darby canine kidney cell line, they segregate to the basolateral and apical membranes, respectively .