Rheological Properties of Southern Pine Oleoresins

Despite the economic and ecologic importance of pine oleoresins, their rheology remains little explored. In this report we describe rheological properties of oleoresins produced by mature trees of four southern pines native to North America (loblolly, slash, longleaf, shortleaf). Results indicate that these oleoresins are structured fluids that exhibit viscoelastic behavior, but differ in flow behavior. Slash pine oleoresin exhibited Newtonian flow behavior while the oleoresin from the longleaf and shortleaf pines showed pseudoplastic behavior and the loblolly pine oleoresin showed Bingham fluid behavior with a yield stress of about 1.980 Pa. Temperature-dependent viscosities for the oleoresin samples studied were well described by the Arrhenius model, yielding flow activation energies ranging from 153.5 to 219.7 kJ/mol. The viscosity of the slash pine oleoresin sample was found to be less sensitive to temperature than that of the shortleaf or longleaf pine samples. The time-temperature superposition principle was successfully applied to pine oleoresins to show behavior over the temperature range of 25 - 65 °C typical for a thermorheologically simple system. Such behavior is consistent with the temperature dependent viscoelastic properties found for these complex fluids, and supports the effective use of rheological evaluations for describing physical properties of pine oleoresins

Basins of Attraction: Population Dynamics with Two Stable 4-cycles

We use the concepts of composite maps, basins of attraction, basin switching, and saddle fly-by\u27s to make the ecological hypothesis of the existence of multiple attractors more accessible to experimental scrutiny. Specifically, in a periodically forced insect population growth model we identify multiple attractors, namely, two locally stable 4-cycles. Using the model-predicted basins of attraction, we examine data time series from a Tribolium experiment for evidence of the multiple attractors. We conclude that the multiple attractor hypothesis together with demographic stochasticity accounts for the experimental observations

Lectin-binding characterizes the healthy human skeletal muscle glycophenotype and identifies disease-specific changes in dystrophic muscle

Our understanding of muscle glycosylation to date has derived from studies in mouse models and a limited number of human lectin histochemistry studies. As various therapeutic approaches aimed at treating patients with muscular dystrophies are being translated from rodent models to human, it is critical to better understand human muscle glycosylation and relevant disease-specific differences between healthy and dystrophic muscle. Here, we report the first quantitative characterization of human muscle glycosylation, and identify differentiation- and disease-specific differences in human muscle glycosylation. Utilizing a panel of 13 lectins with varying glycan specificities, we surveyed lectin binding to primary and immortalized myoblasts and myotubes from healthy and dystrophic sources. Following differentiation of primary and immortalized healthy human muscle cells, we observed increased binding of Narcissus pseudonarcissus agglutinin (NPA), PNA, MAA-II and WFA to myotubes compared to myoblasts. Following differentiation of immortalized healthy and dystrophic human muscle cells, we observed disease-specific differences in binding of NPA, Jac and Tricosanthes japonica agglutinin-I (TJA-I) to differentiated myotubes. We also observed differentiation- and disease-specific differences in binding of NPA, Jac, PNA, TJA-I and WFA to glycoprotein receptors in muscle cells. Additionally, Jac, PNA and WFA precipitated functionally glycosylated α-DG, that bound laminin, while NPA and TJA-I did not. Lectin histochemistry of healthy and dystrophic human muscle sections identified disease-specific differences in binding of O-glycan and sialic acid-specific lectins between healthy and dystrophic muscle. These results indicate that specific and discrete changes in glycosylation occur following differentiation, and identify specific lectins as potential biomarkers sensitive to changes in healthy human muscle glycosylation