On the institution of the moral subject: on the commander and the commanded in Nietzsche's discussion of law

The article discusses how Nietzsche understands the institution of law and morals in distinction to Kant and the Christian tradition. It argues that Nietzsche to a large extent is inspired by the paradigm-shift toward a evolutionary biological thinking introduced by several of his peers in the late 19th century, among else F. A. Lange, who sees this shift as a sobering scientific-materialistic alternative to Kant. In Nietzsche, the Kantian moral imperative is replaced with a notion of a morality emerging thanks to historical, or pre-historical, civilizational processes, imposed on a feebleminded human without any inherent rational dispositions to obey Law. It is also a process, which rather than universalizing the human, splits it in a duality where one part obeys old immediate self-interests and another part obeys new 'commands,' having been shouted 'into the ear' by a so-called 'commander.' The compliance with law takes two radically different forms in Nietzsche: servile and mediocre individuals need to be exposed to discipline and punishment in order to adopt Law; while so-called 'sovereign' individuals are able to impose law upon themselves. The figure of the 'sovereign' has consequently been an issue for vigorous debate in especially the Anglo-Saxon tradition of Nietzsche research, since his apparent 'respect for law' and 'sense of duty' reiterate typical Kantian qualities. Relating to these discussions, I suggest that Nietzsche's 'sovereign' (in one context) is identical his 'commander' (in other contexts). When the 'sovereign' as such imposes law upon himself and others, his act is conventional and arbitrary (like language in Saussure), and is rather irrational than rational as in Kant. His will is not a good will, nor a rational will with a vision of human autonomy. His command of himself and others is a performative, thus without truth-value (like illocutionary speech-acts in Austin and Searle).

The 42-kDa coat protein of Andean potato mottle virus acts as a transcriptional activator in yeast

Interactions of viral proteins play an important role in the virus life cycle, especially in capsid assembly. Andean potato mottle comovirus (APMoV) is a plant RNA virus with a virion formed by two coat proteins (CP42 and CP22). Both APMoV coat protein open reading frames were cloned into pGBT9 and pGAD10, two-hybrid system vectors. HF7c yeast cells transformed with the p9CP42 construct grew on yeast dropout selection media lacking tryptophan and histidine. Clones also exhibited ß-galactosidase activity in both qualitative and quantitative assays. These results suggest that CP42 protein contains an amino acid motif able to activate transcription of His3 and lacZ reporter genes in Saccharomyces cerevisiae. Several deletions of the CP42 gene were cloned into the pGBT9 vector to locate the region involved in this activation. CP42 constructions lacking 12 residues from the C-terminal region and another one with 267 residues deleted from the N-terminus are still able to activate transcription of reporter genes. However, transcription activation was not observed with construction p9CP42deltaC57, which does not contain the last 57 amino acid residues. These results demonstrate that a transcription activation domain is present at the C-terminus of CP42 between residues 267 and 374.

The calcium-dependent protease of Loxosceles gaucho venom acts preferentially upon red cell band 3 transmembrane protein

Eighty micrograms red blood cell (RBC) ghosts from patients who had previously exhibited the cutaneous form of loxoscelism (presenting localized dermonecrosis) and the viscerocutaneous form of loxoscelism (presenting dermonecrosis, hemoglobinuria, hematuria, and jaundice) and from controls were incubated with 2.5 µg crude Loxosceles gaucho venom in 5 mM phosphate buffer, pH 7.4, at 37ºC. Among all membrane proteins, quantitative proteolysis of the important integral transmembrane protein 3 increased with venom dose and with incubation time from 30 to 120 min, as demonstrated by gel densitometry. Similar quantitative data were obtained for RBC ghosts from patients and from control subjects, a fact that argues against the possibility of genetic factors favoring the hemolytic viscerocutaneous form. These data suggest that the clinical forms may be different types of the same disease, with the viscerocutaneous form being the result of large amounts of intravascularly injected venom and the superficial form being the result of in situ venom action. Since protein 3 is a housekeeping integral membrane protein, whose genetic deficiency leads to hemolytic anemia, it is reasonable to relate it to the hemolysis which occurs in the viscerocutaneous form of loxoscelism. The venom protease responsible for the process was not inhibited after 120-min incubation by 0.2 mM paramethylsulfonyl fluoride or by 0.2 mM N-ethylmaleimide but was inhibited by 25 mM ethylenediaminetetraacetic acid (a calcium-chelating agent) in 5 mM phosphate buffer at pH 7.4, which suggests that the enzyme is a calcium-dependent metalloprotease.