Titlebook: Biochemistry of Membrane Transport; FEBS - Symposium No. Giorgio Semenza,Ernesto Carafoli Conference proceedings 1977 Springer-Verlag Berli

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Nonlinearity of Reciprocal Plots in Transport Kineticsf the transport system in the intact cell. The dissociation constant K. of the binding protein-ligand complex is then compared with the half-saturation constant K. of transport and usually found to disagree by one or two orders of magnitude. Some of the reasons for this possible disagreement follow from kinetic considerations.

lymphedema

HARP

The Asymmetry of Sugar Transport in the Red Cell Membraneve been derived from the kinetic equations (Widdas, 1952; Rosenberg and Wilbrandt, 1955; Wilbrandt and Rosenberg, 1961; Stein, 1967). It is fair to say that the great majority of these predictions has been confirmed by experiment. However, there are a few discrepancies that have led to rejection or modification of the basic concept.

commune

AGGER

0172-6625 e of Technology, Zlirich, July 18-23, 1976. Of the speakers invited or­ iginally, only five could not attend the meeting, and of the lectures given, all but one of the texts are published here. Thus, this volume gives a faithful ac­ count of the way the meeting was originally conceived and actually

幼稚

温和女孩

https://doi.org/10.1007/978-3-8349-8473-9ar that a globular “intrinsic” protein (as defined by Singer and Nicolson, 1972) would have a rotational relaxation time at least as slow as microseconds (e.g., see Cherry, 1976). Rhodopsin, which is the only membrane protein whose rotational diffusion has been quantitatively determined, has a relaxation time of 20 μs at 20°C (Cone, 1972).

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pus840

Motional Freedom of Integral Proteins in the Mitochondrial Energy-Transducing Membranembrane transport may find its ultimate complexity in the energy-transducing membrane. Nevertheless, the progress which has occurred over the past twenty years in the elucidation of substrate, ion, and electron transport processes in this membrane has been overwhelming.

过分自信

Rotational Diffusion of Proteins in Membranesar that a globular “intrinsic” protein (as defined by Singer and Nicolson, 1972) would have a rotational relaxation time at least as slow as microseconds (e.g., see Cherry, 1976). Rhodopsin, which is the only membrane protein whose rotational diffusion has been quantitatively determined, has a relaxation time of 20 μs at 20°C (Cone, 1972).