Proteinbiosynthese in Rattenhirnzellkernen

Fleischer-Lambropoulos, H; I, Reinsch

doi:10.1515/bchm2.1971.352.1.593

Cited by 17 publications

(2 citation statements)

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“…Some RNA, probably associated with contaminating rough membranes, was solubilized as indicated by the lowered RNA/DNA ratio (Table 4). With respect to nucleic acids and protein, these effects were in accordance with earlier data (LBVTRUP-REIN and MCEWEN, 1966;BURDMAN and JOURNEY, 1969;FLEISCHER-LAMBROPOULOS and REINSCH, 1971). The effects of treatment with Triton X-100 solutions on the morphology of the nuclei are shown in Figs.…”

Section: Fractionation Of the Nuclei With Detergent And Salt Solutionssupporting

confidence: 91%

“…Comparison of the RNA/DNA and protein/DNA ratios of the homogenates with those of the nuclear fractions (Table 4) showed that the nuclei had considerably lower contents of RNA and protein. For brain nuclei these ratios vary with the method used for isolation (SPORN et al, 1962; LBVTRUP-REIN and MCEWEN, 1966;BALAZS and COCKS, 1967;BURDMAN and JOURNEY, 1969;KEAN, 1970;FLEISCHER-LAMBROPOULOS and REINSCH, 1971 ;AUSTOKER et al, 1972) and with the brain area from which they were prepared (Table 4). The 1.87).…”

Section: Identification and Purity Of The Nucleimentioning

confidence: 99%

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THE SUBCELLULAR LOCALIZATION OF CYTIDINE 5′‐MONOPHOSPHO‐N‐ACETYLNEURAMINIC ACID SYNTHETASE IN CALF BRAIN

Eijnden

1973

Journal of Neurochemistry

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Abstract— The subcellular distribution of cytidine 5′‐monophospho‐N‐acetylneuraminic acid synthetase, which is a key enzyme involved in the biosynthesis of sialo‐glycoproteins and gangliosides, was studied in the frontal grey cortex and the corpus callosum of the calf brain. It appeared that the enzyme was highly concentrated in nuclear fractions, which were shown to be relatively pure as evaluated from morphological, enzymic and chemical data. The possibility that the nuclear localization of the enzyme was due to an artifact, as the result of adsorption onto the nuclear membrane or absorption into the nucleus during the homogenization of the tissue, was ruled out completely and so it appeared that cytidine 5′‐monophospho‐N‐acetylneuraminic acid synthetase, at least for the greater part, is a true nuclear enzyme. The subnuclear localization of the enzyme was shown to be in the nuclear sap. Both neuronal and glial cell nuclei contained the enzyme, which makes it very likely that biosynthesis of sialo‐glycoproteins and/or gangliosides occurs in neurons as well as in glial cells. The significance of the nuclear localization of the enzyme for the biosynthesis of sialic acid containing macromolecules and the possible regulatory role played by the nucleus in this process are discussed.

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Section: Fractionation Of the Nuclei With Detergent And Salt Solutionssupporting

confidence: 91%