Distribution of cytochrome b5 between sonicated phospholipid vesicles of different size.

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Distribution of cytochrome b5 between sonicated phospholipid vesicles of different size.

Cytochrome b5 is an amphipathic integral membrane protein that spontaneously inserts, post-translationally, into intracellular membranes. When added to preformed phospholipid vesicles, it binds in a so-called "loose," or transferable, configuration characterized by the ability of the protein to rapidly equilibrate between vesicles. A heterogeneous dispersion of sonicated phosphatidylcholine ves...

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Changes in the u.v.-visible absorption spectrum of cytochrome b5 which occur upon addition of dicetyl phosphate, dimyristoyl phosphatidic acid (DMPA), or mixed DMPA/dimyristoyl phosphatidylcholine vesicles are consistent with haem transfer from the cytochrome to the membrane via an intermediate haemoprotein species. The effects of vesicle charge and concentration on the kinetics of haem transfe...

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Interaction of non-myristoylated NADH-cytochrome b5 reductase with cytochrome b5-dimyristoylphosphatidylcholine vesicles.

An expression vector for NADH-cytochrome b5 reductase containing a thrombin cleavage site directly before the N-terminal glycine residue of the flavoprotein was used to isolate the non-myristoylated enzyme by thrombin cleavage of the initial fusion protein of a short segment of the multiple cloning site of the plasmid vector and the reductase. This flavoprotein preparation, containing only the ...

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The nonpolar peptide segment of cytochrome b5. Binding to phospholipid vesicles and identification of the fluorescent tryptophanyl residue.

The nonpolar peptide segment of cytochrome b5 consisting of the COOH-terminal 43 amino acid residues binds rapidly to dimyristyl lecithin vesicles above the transition temperature of the phospholipid. The binding is complete as indicated by density gradient centrifugation and is accompanied by approximately a 2-fold increase in the fluorescence emission of the protein, and insertion in the bila...

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Frequency dependence of 31P NMR linewidths in sonicated phospholipid vesicles: effects of chemical shift anisotropy.

Phosphorus nuclear magnetic resonance (3’P NMR) is an increasingly important physical technique for the elucidation of structural features of phospholipid bilayer membranes [l-S] . In sonicated vesicles, however, the chemical shift differences between different classes of phospholipids are of approximately the same magnitude as the widths of the resonances themselves [5,6]. For many application...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1985

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)88909-8