Economic voting and electoral volatility in Turkish provinces

Two groups of questions were addressed in this paper: (1) Is voter punishment of the incumbent the primary factor in electoral volatility? Are there any other types of vote swings that underlie volatility? (2) In general, does a decline in economic growth destabilize voter behavior? If so, what kinds of vote swings does an economic downturn tend to generate? Provincial-level panel data analysis yielded the following results: (1) Changes in volatility is primarily due to vote swings from the incumbent to the opposition and also to and from left-wing and right-wing parties. (2) Lower economic growth increases electoral volatility. Economic decline induces vote swings not only from the government to the opposition but also from left-wing to right-wing parties. This is probably because right-wing parties seem more concerned with economic issues and are thus more popular than left-wing parties with lower-income voters.

Fratris Petri de Aragon, Ordinis Eremitarum Sancti Augustini, ... In Secundam Secundæ Diui Thomæ Doctoris Angelici commentariorum, tomus primus ...

Colofón en 3F7v

Fratris Petri de Aragon, Ordinis Eremitarum Sancti Augustini, ... In Secundam Secundæ Diui Thomæ Doctoris Angelici commentariorum, tomus primus ...

Colofón en 3F7v

Diuini vatis Abbatis Ioachim liber co[n]cordie noui ac veteris Testamenti : nunc primo impressus [et] in luce[m] editus : Opus equidem diuinum ac aliorum fere omnium tractatuum ...

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O instituto da licitação no direito francês

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Membrane disposition of the M5-M6 hairpin of Na+,K(+)-ATPase alpha subunit is ligand dependent.

Extensive proteolytic digestion of Na+,K(+)-ATPase (EC 3.6.1.37) by trypsin produces a preparation where most of the extramembrane portions of the alpha subunit have been digested away and the beta subunit remains essentially intact. The fragment Gln-737-Arg-829 of the Na+,K(+)-ATPase alpha subunit, which includes the putative transmembrane hairpin M5-M6, is readily, selectively, and irreversibly released from the posttryptic membrane preparation after incubation at 37 degrees C for several minutes. Once released from the membrane, the fragment aggregates but remains water soluble. Occlusion of K+ or Rb+ specifically prevents release of the Gln-737-Arg-829 fragment into the supernatant. Labeling of the posttryptic membrane preparation with cysteine-directed reagents revealed that Cys-802 (which is thought to be located within the M6 segment) is protected against the modification by Rb+ while this fragment is in the membrane but can be readily modified upon release. Cation occlusion apparently alters the folding and/or disposition of the M5-M6 fragment in the membrane in a way that does not occur when the fragment migrates to the aqueous phase. The ligand-dependent disposition of the M5-M6 hairpin in the membrane along with recent labeling studies suggest a key role for this segment in cation pumping by Na+,K(+)-ATPase.