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Transport of Multiple Enzymes through Semipermeable Membrane and Effect of Surfactants

C. Trigo, S.W. Leung, A. Bhushan, C.K. Daniels and J.C.K. Lai
Idaho State University, College of Engineering, US

multiple enzymes, membrane, transport, surfactant

Surfactants are known to influence functions of many proteins in membranes, cells and tissues. Because most studies to elucidate the effects of surfactants on membrane-bound proteins and cells employed heterogeneous or complex systems, it is difficult to extrapolate the results of such studies to delineate the effects of surfactants on a single protein. We therefore systematically investigated how anionic surfactants of different hydrophilicities affected three metabolically important enzymes (namely, glutamate dehydrogenase (GDH), lactate dehydrogenase (LDH), and malate dehydrogenase (MDH)) of various molecular masses at a pH range relevant to body functions (6.5-7.4).
For the four anionic surfactants used in this study, there seemed to be a pH dependence on how hydrophilicity would affect single cellar protein transfer (across the membrane).
For the three enzymes with all the surfactant used in this study at pH 6.95, the amount of normalized mass transferred across a semipermable membrane was consistently in the same descending order: LDH, GDH, and MDH.
For multiple enzymatic protein transport, with and without surfactants, mass transfer of protein across a semipermeable membrane appeared not to follow conventional diffusional concept. Our previous results indicated that multiple factors would influence the amount of mass permeated through the membrane; the effect of those factors are more complex with the addition of surfactant, which would have strong implications in cellar signaling.

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