Lipid binding to the amphipathic membrane protein cytochrome b5

dc.contributor.authorDehlinger, P. J.
dc.contributor.authorJost, P. C.
dc.contributor.authorGriffith, O. H.
dc.date.accessioned2016-05-25T23:22:08Z
dc.date.available2016-05-25T23:22:08Z
dc.date.issued1974-06
dc.description6 pagesen_US
dc.description.abstractABSTRACT The lipid hinding properties of the membrane protein cytochrome b:. (detergent-extracted from calf liver microsomal preparations) were characterized by studying the interaction of spin-labeled lipid,- (5-, 12-, and 16-doxylstcaric acid and 5- and 16-cloxylphosphatidylcholine, where cloxyl refers to the nitroxide moiety) with cytochrome b :, using electron "pin resonance spectroscopy. The intact cytochrome b, n1olec11lc immobilizes all of the lipid spin label,;, while the segment of cytochrome b, released by trypsin doei. not afTcct lipid mobility. The immobilization of lipid spin label,-; on the h) ·drophohic surface of intact cytochrome b:, is not appreciably altered by associating the protein with liposomc" · DHTcrcnccs in polarity of the lipid binding site" between c, ·tochromc b, and phospholipid vc,.icles were also ob,-cr\'ed. The lipid binding sites on cytochrome b.; arc hydrophobic by conventional criteria, but arc more polar than the interior of fluid phospholipid bilayers.en_US
dc.identifier.citationDehlinger, P. J., Jost, P. C. & Griffith, O. H. (1974) Lipid binding to the amphipathic membrane protein cytochrome b5. Proc. Natl. Acad. Sci. USA 71, 2280‑2284.en_US
dc.identifier.urihttps://hdl.handle.net/1794/19890
dc.language.isoen_USen_US
dc.publisherProceedings of the National Academy of Sciencesen_US
dc.rightsCreative Commons BY-NC-ND 4.0-USen_US
dc.titleLipid binding to the amphipathic membrane protein cytochrome b5en_US
dc.typeArticleen_US

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