899 resultados para Marius, Gaius, ca. 157-86 B.C.


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Last two leaves blank.

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Bibliography : p. xv; "Works of reference" : p. xl.

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Mode of access: Internet.

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Tr. of: Africa.

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Mode of access: Internet.

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Mode of access: Internet.

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Mode of access: Internet.

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On double leaves, oriental style, in case.

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Este artículo analiza la existencia de un posible ritual en la antigua Macedonia que fuese similar al Akîtu babilonio. Pensamos que la victoria de Zeus sobre sus enemigos en la gigantomaquia y tifonomaquia fue celebrada por los reyes macedonios para fortalecer su posición en el poder. Aunque no hay evidencias directas de ello, tenemos una serie de diferentes fuentes en las cuales los macedonios están relacionados directa o indirectamente con Tifón y los gigantes. Además, la estratégica importancia del monte Olimpo para los macedonios nos hace pensar que la victoria de Zeus sobre las fuerzas del mal fue conmemorada de alguna forma por ellos.

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Quintus Curtius found in his sources a speech where a Scythian censured Alexander, followed by the King’s reply. Curtius drastically abridged this second discourse in order to highlight the criticism of the Macedonian. The Scythian’s words have a striking rhetorical language and some allusions taken from Greek literature, in addition to possible indirect references to Caligula. Curtius declares that he follows his source word-for-word aiming to justify these inconsistencies, but also trying to hide the manipulations he has done to achieve his own narrative purposes.

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$\rm Ca\sp{2+}$-dependent exposure of an N-terminal hydrophobic region in troponin C (TnC) is thought to be important for the regulation of contraction in striated muscle. To study these conformational changes in cardiac troponin (cTnC), the $\varepsilon$C and $\varepsilon$H chemical shifts for all 10 Met residues in cTnC were sequence-specific assigned on NMR spectra using a combination of two dimensional NMR techniques and site-directed mutagenesis. The assigned methyl-Met chemical shifts were used as structural markers to monitor conformational changes induced by $\rm Ca\sp{2+}.$ The results showed that binding of $\rm Ca\sp{2+}$ to the regulatory site in the N-domain induced large changes in the $\varepsilon$H and $\varepsilon$C chemical shifts of Met 45, Met 80, Met 81 in the predicted N-terminal hydrophobic region, but had no effect on the chemical shifts of Met residues located in the C-domain. These results suggest that the $\rm Ca\sp{2+}$-dependent functions of cTnC are mainly through N-terminal domain of cTnC.^ To further define the molecular mechanism by which TnC regulates muscle contraction, single Cys residues were engineered at positions 45, 81, 84 or 85 in the N-terminal hydrophobic region of cTnC to provide sites for attachment of specific blocking groups. Blocking groups were coupled to these Cys residues in cTnC mutants and the covalent adducts were tested for activity in TnC-extracted myofibrils. Covalent modification of cTnC(C45) had no effect on maximal myofibril ATPase activity. Greatly decreased myofibril ATPase activity resulted when the peptide or biotin was conjugated to residue 81 in cTnC(C81), while less inhibition resulted from covalent modification of cTnC(C84) or cTnC(C85). The results suggest that limited sites of the N-terminal hydrophobic region in cTnC are important for transducing the $\rm Ca\sp{2+}$ signal to troponin I (TnI) and are sensitive to modification, while other regions are less important or can adapt to steric hindrances introduced by bulky blocking groups.^ Although the exposed TnI interaction site in the N-terminal hydrophobic region of TnC is crucial for function of TnC, other regions in the N-domain of TnC may also participate in transducing the $\rm Ca\sp{2+}$ signal and conferring the maximal activation of actomyosin ATPase. The interactions between the B-/C-helices of cTnC and cTnI were characterized using a combination of site-directed mutagenesis, fluorescence and covalent modification. The results suggest that the $\rm Ca\sp{2+}$-dependent interactions of the B-/C-helices of cTnC with TnI may be required for the maximal activation of muscle contraction. ^