PMID: 6165584Apr 1, 1981Paper

Synthesis and insertion, both in vivo and in vitro, of rat-liver cytochrome P-450 and epoxide hydratase into Xenopus laevis membranes

European Journal of Biochemistry
R I OhlssonF P Guengerich

Abstract

We described whole cell and cell-free systems capable of inserting into membranes cytochrome P-450 and epoxide hydratase made under the direction of rat liver RNA. The systems have been used to study the pathways followed by newly made secretory and integral membrane proteins. The cell-free system contains Xenopus laevis embryo membranes, and demonstrates competition for a common receptor between cytochrome P-450 and epoxide hydratase, and normal secretory proteins: evidence is provided for differential membrane receptor affinity. Thus, synthesis of secretory and membrane proteins appears to involve a common initial pathway. Microinjection of rat liver RNA into whole oocytes suggests that membrane insertion is neither cell type nor species specific, because functional rat liver enzymes are found inserted in the endoplasmic reticulum of the frog cell. Nonetheless, insertion is highly selective since albumin and several other proteins made under the direction of the injected liver RNA are sequestered within membrane vesicles and are then secreted by the oocyte, whilst epoxide hydratase and cytochrome P-450 are inserted into membranes but are not secreted.

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Citations

Jan 1, 1989·International Journal of Developmental Neuroscience : the Official Journal of the International Society for Developmental Neuroscience·R F AldersonE T Butler
Jan 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·C B GundersenR Miledi
Apr 27, 2016·The Journal of Membrane Biology·Carlos A Báez-PagánJosé A Lasalde-Dominicci
Jan 1, 1985·CRC Critical Reviews in Biochemistry·H Soreq
Jul 13, 2004·The Journal of Biological Chemistry·Gretchen Y López-HernándezJosé A Lasalde-Dominicci

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