Biomaterial Database

The interaction of the membrane binding segment of cytochrome b5 with phospholipid vesicles. A pulse-radiolysis investigation. 1981

F Pochon, and V Favaudon, and C Ferradini, and J Pucheault

The reactions of the radical anions Br2- and (SCN)2- produced by pulse-radiolysis have been used to study the interaction of dipalmitoyl phosphatidyl choline vesicles with the membrane binding segment (MBS) of cytochrome b5. Tryptophan oxidation by Br2- at neutral pH was characterized spectrophotometrically in detergent-solubilized solutions of MBS; the attack of tyrosine by (SCN)2- under alkaline conditions could also be observed directly. The incorporation of MBS into the lipid bilayer protected the tryptophan, tyrosine and methionine residues from oxidation by Br2- or (SCN)2-. Some structural implications of these results are discussed.

UI	MeSH Term	Description	Entries
D008081	Liposomes	Artificial, single or multilaminar vesicles (made from lecithins or other lipids) that are used for the delivery of a variety of biological molecules or molecular complexes to cells, for example, drug delivery and gene transfer. They are also used to study membranes and membrane proteins.	Niosomes,Transferosomes,Ultradeformable Liposomes,Liposomes, Ultra-deformable,Liposome,Liposome, Ultra-deformable,Liposome, Ultradeformable,Liposomes, Ultra deformable,Liposomes, Ultradeformable,Niosome,Transferosome,Ultra-deformable Liposome,Ultra-deformable Liposomes,Ultradeformable Liposome
D011663	Pulmonary Surfactants	Substances and drugs that lower the SURFACE TENSION of the mucoid layer lining the PULMONARY ALVEOLI.	Surfactants, Pulmonary,Pulmonary Surfactant,Surfactant, Pulmonary
D011675	Pulse Radiolysis	Use of a pulse of X-rays or fast electrons to generate free radicals for spectroscopic examination.	Radiolysis, Pulse
D003580	Cytochromes	Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands.	Cytochrome
D015786	Cytochromes b5	Cytochromes of the b group that are found bound to cytoplasmic side of ENDOPLASMIC RETICULUM. They serve as electron carrier proteins for a variety of membrane-bound OXYGENASES. They are reduced by the enzyme CYTOCHROME-B(5) REDUCTASE.	Apocytochrome b5,Cytochrome b-5,Cytochrome b5,Ferricytochrome b5,Cytochrome b 5