Enzyme and phospholipid asymmetry in liver microsomal membranes.

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Enzyme and phospholipid asymmetry in liver microsomal membranes

The transverse distribution of enzyme proteins and phospholipids within microsomal membranes was studied by analyzing membrane composition after treatment with proteases and phospholipases. Upon trypsin treatment of closed microsomal vesicles, NADH- and NADPH-cytochrome c reductases as well as cytochrome b5 were solubilized or inactivated, while cytochrome P-450 was partially inactivated. When ...

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Phospholipid asymmetry in rough- and smooth-endoplasmic-reticulum membranes of untreated and phenobarbital-treated rat liver.

Phospholipase C was used as a probe for the distribution of phospholipids about the membrane of rough and smooth microsomal fractions from normal and phenobarbital-treated rat liver. All membranes exhibited an asymmetric distribution, with phosphatidylethanolamine and phosphatidylserine concentrated in the inner leaflet of the bilayer and phosphatidylcholine and sphingomyelin concentrated in th...

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Heterogeneity of Rough-surfaced Liver Microsomal Membranes

Rough microsomes from the livers of adult, phenobarbital-treated, and newborn rats were subfractionated on a continuous sucrose gradient. Among the subfractions a marked heterogeneity in the distribution patterns of some enzyme activities appears. The isopycnic density of the various fractions in aqueous sucrose ranges from 1.17 to 1.25. The sedimentation coefficients (so) in 0.25 M sucrose lie...

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Compartmentalization of phosphatidylethanolamine in microsomal membranes from rat liver.

Microsomal membranes from rat liver were treated with the cross-linking reagent 1,5-difluoro-2,4-dinitrobenzene (DFDNB). Experimental work showed that at a probe concentration of 0.75 mM all free phosphatidylethanolamine (PE) and phosphatidylserine (PS) were found as dinitrophenyl derivatives: 29% of PE was in monomeric form, 9% dimeric, 2% interacted with PS, and 63% cross-linked to protein. P...

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Role of phospholipid in electron transfer in a reconstituted liver microsomal enzyme system containing cytochrome P-450.

The enzyme system in liver microsomes which catalyzes the hydroxylation of fatty acids, hydrocarbons and a variety of drugs and other foreign compounds has been resolved into 3 components. These are: (a) a solubilized form of cytochrome P-450, (b) a solubilized form of NADPH-cytochrome P-450 reductase, and (c) a heat-stable component which has the solubility properties of a lipid. All 3 compone...

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ژورنال

عنوان ژورنال: Journal of Cell Biology

سال: 1977

ISSN: 0021-9525,1540-8140

DOI: 10.1083/jcb.72.3.568