Making and breaking order via clothing Clothing regulation, cross-dressing, and the ordering mentality in later medieval and early modern England

Following the events which disrupted social stability in fourteenth and fifteenth-century England, individuals from a variety of social contexts demonstrated a particular necessity to see order visibly displayed in society. This thesis examines sumptuary regulations and cross-dressing side by side to demonstrate clothing's relationship to both making and breaking order. In the act of revealing this relationship, this thesis will argue that the two cases demonstrate clothing’s importance in creating a visible confirmation of social order which ultimately brings to the surface an underlying collective ordering mentality that equated a sense of security with arranging everyone in society in their rightful place

Ethanol stimulates expression of functional H+,K+-ATPase in SF9 cells

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Role of sugar residues for recombinant gastric H+,K+-ATPase

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Cholecystokinin-stimulated enzyme secretion from dispersed rabbit pancreatic acinar cells : phosphorylation-dependent changes in potency and efficacy

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Differences in uptake, storage and release properties between inositol trisphosphate-sensitive and -intensitive Ca2+ stores in permeabilized pancreatic acinar cells

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Involvement of glutamic acid 820 in K+ and SCH 28080 binding to gastric H+,K+-ATPase

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Electrophysiological analysis of the mutated Na,K-ATPase cation binding pocket.

Contains fulltext : 142631.pdf (Publisher’s version ) (Open Access)Na,K-ATPase mediates net electrogenic transport by extruding three Na+ ions and importing two K+ ions across the plasma membrane during each reaction cycle. We mutated putative cation coordinating amino acids in transmembrane hairpin M5-M6 of rat Na,K-ATPase: Asp776 (Gln, Asp, Ala), Glu779 (Asp, Gln, Ala), Asp804 (Glu, Asn, Ala), and Asp808 (Glu, Asn, Ala). Electrogenic cation transport properties of these 12 mutants were analyzed in two-electrode voltage-clamp experiments on Xenopus laevis oocytes by measuring the voltage dependence of K+-stimulated stationary currents and pre-steady-state currents under electrogenic Na+/Na+ exchange conditions. Whereas mutants D804N, D804A, and D808A hardly showed any Na+/K+ pump currents, the other constructs could be classified according to the [K+] and voltage dependence of their stationary currents; mutants N776A and E779Q behaved similarly to the wild-type enzyme. Mutants E779D, E779A, D808E, and D808N had in common a decreased apparent affinity for extracellular K+. Mutants N776Q, N776D, and D804E showed large deviations from the wild-type behavior; the currents generated by mutant N776D showed weaker voltage dependence, and the current-voltage curves of mutants N776Q and D804E exhibited a negative slope. The apparent rate constants determined from transient Na+/Na+ exchange currents are rather voltage-independent and at potentials above -60 mV faster than the wild type. Thus, the characteristic voltage-dependent increase of the rate constants at hyperpolarizing potentials is almost absent in these mutants. Accordingly, dislocating the carboxamide or carboxyl group of Asn776 and Asp804, respectively, decreases the extracellular Na+ affinity

Phosphorylation and desensitization of the pancreatic cholecystokinin-A receptor

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The beta-subunits of Na+,K+-ATPase and gastric H+,K+-ATPase have a high preference for their own alpha-subunit and affect the K+ affinity of these enzymes

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