999 resultados para Hoar, E. R. (Ebenezer Rockwood), 1816-1895.


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Ulysses S. Grant, Schuyler Colfax, James G. Blaine, Hamilton Fish, John A. Rawlins, Jacob D. Cox, George S. Boutwell, Adolph E. Borie, John A.J. Creswell, Ebenezer R. Hoar.

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بسم الله الرحمن الرحيم وبه ثقتي حمد العلام اجدي ذوي الافهام بتحقيق دقايق اللغات ... :Incipit

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The alpha subunits of the heterotrimeric guanine nucleotide-binding proteins (G proteins) hydrolyze GTP at a rate significantly higher than do most members of the Ras family of approximatelly 20-kDa GTP-binding proteins, which depend on a GTPase-activating protein (GAP) for acceleration of GTP hydrolysis. It has been demonstrated that an inserted domain in the G-protein alpha subunit, not present in the much smaller Ras-like proteins, is responsible for this difference [Markby, D. W., Onrust, R. & Bourne, H. R. (1993) Science 262, 1895-1900]. We report here that ARD1, a 64-kDa protein with an 18-kDa carboxyl-terminal ADP-ribosylation factor (ARF) domain, exhibited significant GTPase activity, whereas the ARF domain, expressed as a recombinant protein in Escherichia coli, did not. Addition of the 46-kDa amino-terminal extension (similarly synthesized in E. coli) to the GTP-binding ARF-domain of ARD1 enhanced GTPase activity and inhibited GDP dissociation. The kinetic properties of mixtures of the ARF and non-ARF domains were similar to those of an intact recombinant ARD1. Physical association of the two proteins was demonstrated directly by gel filtration and by using the immobilized non-ARF domain. Thus, like the alpha subunits of heterotrimeric G proteins, ARD1 appears to consist of two domains that interact to regulate the biological activity of the protein.

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Title from spine.

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Cover title.

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v.1.Iugo & Ingraben.-v.2.Das nest der zaunkönige.-v.3.Die brder vom deutschen hause.-v.4.Marcus König.-v.5.Die geschwister.-v.6.Aus eine kleine stadt.

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Contiene: Vol. 1.

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Contiene: t. 1-2, t. 3-4, t. 5-6, t. 7-8. t-. 9-10.

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Texto impreso en letra gotica.

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Contiene: Vol. I - Vol. II - Vol. III - Vol. IV.

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Contiene: vol. 1.

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Mode of access: Internet.

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Mode of access: Internet.