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At least 631 records · Page 35Linked to original sources
PubMed1977

Subcellular fractionation by differential and zonal centrifugation of the trypanosomatid Crithidia fasciculata.

Homogenates of Crithidia fasciculata were fractionated by differential centrifugation. Mitochondria were sedimented quantitatively at 10(4) g-min and accounted for approximately 10% of the total recovered protein. Catalase was found exclusively in the supernatant fraction whilst NADH:cytochrome c oxidoreductase and p-nitrophenylphosphatase were found in all the fractions. Zonal centrifugation confirmed that catalase was non-sedimentable. Clean separation of mitochondria was obtained in both high-speed and rate zonal experiments, but no NADH:cytochrome c oxidoreductase activity could be detected in these organelles. Separation of large lysosomal vacuoles which contained p-nitrophenylphosphatase activity was obtained and these were clearly resolved from mitochondria by both high-speed and rate zonal centrifugation.

Cell Fractionation↗
PubMed1987

Locations of the hydrogenases of Methanobacterium formicicum after subcellular fractionation of cell extract.

The F420 hydrogenase of Methanobacterium formicicum was associated with membranes isolated by sucrose density gradient ultracentrifugation of cell extract. The methyl viologen hydrogenase was present in the soluble fractions. Column chromatography with phenyl-Sepharose CL-4B revealed that the F420 hydrogenase was strongly hydrophobic, suggesting that it associates with isolated membranes through hydrophobic interactions.

Cell Fractionation↗
PubMed1991

Distribution of polyamine oxidase activity in rat tissues and subcellular fractions.

The activity of polyamine oxidase (PAO) in rat tissues, and its subcellular distribution, were assayed using a simple polarographic method. The highest PAO activity was measured in the liver and the lowest in the skeletal muscle. In liver, kidney and uterus the highest specific PAO activity was found in the light mitochondrial fraction. PAO was not found in the microsomal fraction except in the kidney.

Animals↗
PubMed1979

Melanoma development from subcellular fractions.

Amelanotic melanoma cells, RPMI-1846, were disrupted by sonic energy which caused cell membrane disruption, thereby allowing liberation of viable cellular organelles. These subcellular particles were injected into syngeneic Syrian and nonsyngeneic hamsters in six separate experiments to determine their possible growth potential. A sizable number of the injected hamsters subsequently died as a result of melanoma. In an attempt to be as certain as possible that no whole melanoma cells were injected with sonicated melanoma material, various techniques were used including collodian sections for debris analysis, phase microscopy and electron microscopy. Results of this study suggested that melanoma can be induced from particles within the melanoma cell which are liberated following cell membrane disruption. It appears that a mechanism exists for the transfer of oncogenic information that may not be dependent upon the presence of intact cells or require the participation of a viral agent.

Abdominal Muscles↗
PubMed1981

Subcellular fractionation of alcohol and aldehyde dehydrogenase in the rat testicles.

The subcellular distribution of the enzymes primarily involved in the metabolism of ethanol and acetaldehyde were made in the rat testis and in the epididymis. The enzymes measured were alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). They were NAD-dependent, temperature sensitive and displaying maximal activity in the presence of pyrophosphate buffer at pH 9.8. Both enzymes were readily measurable in the 10% (w/v) testicular and epididymal homogenates. The ADH activity was mainly localized in the nuclear and in the cytosolic fractions of the testis compared to the absence of measurable ADH activity in the epididymis. Testicular ALDH was measurable in all subcellular preparations, i.e. in the nuclear, in the mitochondrial, in the cytosolic and in the microsomal fractions. Maximal testicular ALDH activity was determined in both the nuclear and the cytosolic components compared to a lower microsomal ALDH activity. Determination of Km shows that cytosolic ALDH possesses the lowest apparent Km as contrasted with a high value for the mitochondrial ALDH. Testicular cytosolic ADH but not ALDH was noncompetitively inhibited by 3-methoxytyramine, histamine and d-amphetamine in vitro.

Alcohol Dehydrogenase↗
PubMed1989

Quantitative analysis of phospholipids and demonstration of plasmalogen in human neutrophil subcellular fractions by high-performance liquid chromatography.

The subcellular distribution of phospholipids in unstimulated neutrophils was investigated by high-performance liquid chromatography of lipid extracts of granule and plasma membranes obtained from Percoll density gradients. The mobile phase contained acetonitrile:methanol:85% phosphoric acid (131:3:0.8 v/v/v). Post-nuclear supernatants contained 2.3 micrograms lipid phosphorus/mg protein. Phosphatidylinositol, phosphatidylserine, phosphatidylethanolamine and phosphatidylcholine were demonstrated in azurophil granules, specific granules and in a combined fraction of secretory granules and plasma membranes. Separate estimates of each phospholipid class by peak areas obtained by high-performance liquid chromatography showed that secretory granules and plasma membranes contained most of the phosphatidylinositol and phosphatidylcholine (p less than 0.005 vs peaks areas obtained in azurophil and specific granules), whereas a major part of the phosphatidylethanolamine was located in the specific granules (p less than 0.005 vs peak areas obtained in azurophil granules, and plasma membrane and secretory granules). High-performance liquid chromatography proved to be a useful principle for the demonstration of plasmalogen because the acidic solvent caused hydrolysis of phosphatidalethanolamine, which was recovered as lysophosphatidylethanolamine. Additionally, sphingomyelin was demonstrated in all subfractions by thin-layer chromatography.

Cell Membrane↗