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At least 865 records · Page 48Linked to original sources
PubMed1987

Isolation, characterization and phospholipid composition of lamellar bodies and subcellular fractions from dog lung.

1. Lamellar body fractions from dog lung can be separated by a procedure based on differential centrifugation before ultracentrifugation onto a discontinuous sucrose gradient. This fraction yields about 1% of total protein from the homogenate. 2. The different fractions obtained in the isolation were assayed for the measurement of four subcellular marker enzymes: beta-N-acetylglucosaminidase, acid phosphatase, 5'-nucleotidase and succinate dehydrogenase. 3. Lamellar bodies were not contaminated by mitochondria (0.7 succinate dehydrogenase relative specific activity), whereas high specific hydrolase activities were found (beta-N-acetylglucosaminidase and 5'-nucleotidase were enriched 1.8- and 2.8-fold, respectively). 4. The chemical criterion was established by measuring the specific components of lamellar bodies. The lamellar bodies have the highest phospholipid/protein ratio (0.35); cholesterol/protein ratio (0.15) and the highest phosphatidylglycerol percentages (7.9%). 5. The phospholipid composition of lamellar bodies is distributed among phosphatidylcholine (64.5%), phosphatidylethanolamine (11%), phosphatidylglycerol (7.9%), sphingomyelin (4%), phosphatidylserine and phosphatidylinositol (3%), respectively. The remainder were considered as trace amounts (less than 1%).

Animals↗
PubMed1979

Phospholipase activities in subcellular fractions of human platelets.

A homogenate of human platelets was fractionated by zonal ultracentrifugation into membranes, various granules and mitochondria. The membrane fraction was composed of two populations. The first, which represented 75% of the proteins, was rich in plasma membranes; the second, which represented the remaining 25%, was rich in microsomal membranes. Lysophospholipase was essentially localised in the cytosol. Phospholipase A1 which was only weakly bound to membranes, was mostly found in the soluble fraction (75%); the remainder was located in the plasma membranes and the mitochondria. Two-thirds of the phospholipase A2 was found in the particulate fractions.

Adult↗
PubMed1984

Concanavalin A binding glycoproteins in subcellular fractions from the developing rat cerebral cortex.

Synaptic plasma membrane (SPM) and mitochondrial fractions were prepared from 3-50-day rat cerebral cortex and their purity assessed. The fractions were subjected to electrophoresis on slab gels, stained for protein, and overlaid with 125I-concanavalin A (ConA). ConA binding glycoproteins (CABGs) were revealed by autoradiography. In the SPM fraction CABGs of MW 25,000, 63,000, 80,000, 115,000, 174,000, and 239,000 increased while those of MW 47,000, 75,000, and 190,000 decreased developmentally. In the mitochondrial fraction, CABGs of MW 25,000, 44,000, 115,000 and 174,000 increased while those of 34,000, 43,000, 47,000, 51,000, 80,000, 107,000, and 195,000 decreased developmentally. CABGs of MW 32,000, 63,000, 88,000, 153,000, 190,000, and 239,000 appear to be unique to the SPM fraction and those of MW 34,000, 107,000, and 195,000 are unique to the mitochondrial fraction.

Aging↗