Dehlinger, P. J.Jost, P. C.Griffith, O. H.2016-05-252016-05-251974-06Dehlinger, 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.https://hdl.handle.net/1794/198906 pagesABSTRACT 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-USCreative Commons BY-NC-ND 4.0-USArticle