0000000000352625
AUTHOR
Maria Salmela
Fate of Oxygen in Industrial Oxygen-Alkali Delignification of Softwood Kraft Pulp
Description of kraft cooking and oxygen–alkali delignification of bamboo by pulp and dissolving material analysis
Abstract The oxygen delignification of two bamboo ( Bambusa procera ) kraft pulps with kappa numbers of 13.6 and 20.0 were studied under typical conditions. Based on detailed analysis data on both the kraft and oxygen-delignified pulps and the corresponding spent liquors (black liquors and oxygen stage effluents), three yield and four selectivity estimation methods, utilizing component material balances, were tested resulting in the value ranges 96.2–97.9% and 43.5–60.4%, respectively, for oxygen delignification process studied. The traditional selectivity using the viscosity and kappa number relation was 66.9–68.4%. The studied bamboo kraft pulps behaved typically as birch kraft pulps duri…
Novel α2β1 integrin inhibitors reveal that integrin binding to collagen under shear stress conditions does not require receptor preactivation.
The interaction between α2β1 integrin (GPIa/IIa, VLA-2) and vascular collagen is one of the initiating events in thrombus formation. Here, we describe two structurally similar sulfonamide derivatives, BTT-3033 and BTT-3034, and show that, under static conditions, they have an almost identical effect on α2-expressing CHO cell adhesion to collagen I, but only BTT-3033 blocks platelet attachment under flow (90 dynes/cm(2)). Differential scanning fluorimetry showed that both molecules bind to the α2I domain of the recombinant α2 subunit. To further study integrin binding mechanism(s) of the two sulfonamides, we created an α2 Y285F mutant containing a substitution near the metal ion-dependent ad…
Molecular mechanism of α2β1 integrin interaction with human echovirus 1
Conformational activation increases the affinity of integrins to their ligands. On ligand binding, further changes in integrin conformation elicit cellular signalling. Unlike any of the natural ligands of alpha2beta1 integrin, human echovirus 1 (EV1) seemed to bind more avidly a 'closed' than an activated 'open' form of the alpha2I domain. Furthermore, a mutation E336A in the alpha2 subunit, which inactivated alpha2beta1 as a collagen receptor, enhanced alpha2beta1 binding to EV1. Thus, EV1 seems to recognize an inactive integrin, and not even the virus binding could trigger the conformational activation of alpha2beta1. This was supported by the fact that the integrin clustering by EV1 did …