Abstract
The cell-free protein synthesis by the postmitochondrial supernatant from chicken cerebrum was twofold greater than protein synthesis by the cerebellum or optic lobes. Ribosomal aggregation of mRNA and ribonuclease activity of the postmitochondrial supernatant from the three brain regions was not statistically different. The higher protein synthetic activity of the cerebral postmitochondrial supernatant was associated with both the postribosomal supernatant (cell sap) and microsomal fractions. Cerebral monomeric ribosomes were more active in polyuridylic acid directed polyphenylalanine synthesis than monomeric ribosomes from either the cerebellum or optic lobes. The ability of cerebral cell sap to support polyuridylic acid directed polyphenylalanine synthesis was 1.6 to 2 times greater than cell sap from the other two regions. Cell sap factors other than tRNAphe or phenylalanyl-tRNA synthetases appear to be responsible for the higher protein synthetic activity of the cbr cell sap.
Similar content being viewed by others
References
Furst, S., Lajtha, A., andWaelsch, H. 1958. Amino acid and protein metabolism of the brain. III. Incorporation of lysine into the proteins of various brain areas and their cellular fractions. J. Neurochem. 2:216–225.
Krawczynski, J., Wiszniowska, S., andDrewnowska, I. 1960. Incorporation of radioactivity into proteins of the cerebrum, cerebellum, and other organs after injection of35S in the form of sodium sulphate. J. Neurochem. 5:190–113.
Jarlstedt, J. 1972. Experimental alcoholism in rats: Protein synthesis in subcellular fractions from cerebellum, cerebral cortex and liver after long term treatment. J. Neurochem. 19:603–608.
Richardson, A., McGrown E., Henderson, M., andSwan, P. B. 1971.In vitro amino acid incorporation by the postmitochondrial supernatant from rat liver. Biochem. Biophys. Acta 254:468–477.
Liu, D. S. H., Yang, J. W., andRichardson, A. 1975. Characterization of anin vitro protein synthesis system from the cerebrum, cerebellum, and optic lobes of chick brain, Trans. Ill. State Acad. Sci. 68:2–13.
Gilbert, B., andJohnson, T. 1972. The use of aminoacyl-tRNA to measure polypeptide synthesis by ribosomes isolated from neonatal and adult mouse brain tissue. Biochem. Biophys. Res. Commun. 46:2034–2039.
Solymosy, F. 1968. A new method based on the use of diethyl pyrocarbonate as a nuclease inhibitor for the extraction of undergraded nucleic acid from plant tissue. Eur. J. Biochem. 5:520–527.
Solymosy, F., Lazar, G., andBagi, G. 1970. An improved version of the diethyl pyrocarbonate method for extracting ribosomal nucleic acids. Anal. Biochem. 38:30–45.
Fedorcsak, I., andEhrenberg, L. 1966. Effect of diethyl pyrocarbonate and methyl methanesulfonate on nucleic acids and nucleases. Acta Chem. Scand. 20:107–112.
Layman, D. K., Ricca, G. A., andRichardson, A. 1976. The effect of age on protein synthesis and ribosome aggregation to messenger RNA in rat liver. Arch. Biochem. Biophys. 173:246–254.
Lowry, O., Rosebrough, N., Forr, A., andRandall, R. 1951. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193:265.
Munro, H., andFleck, A. 1966. Recent developments in the measurement of nucleic acids in biological materials. Analyst 91:78–88.
Murthy, M. R. V. 1966. Protein synthesis in growing rat tissue: II. Polyribosome concentration of brain and liver as a function of age. Biochim. Biophys. Acta 119:599–613.
Yamagami, S., andMori, K. 1970. Changes in polysomes in the developing rat brain. J. Neurochem. 17:721–731.
Stenzel, K. H., Aronson, R. F., andRubin, A. L., 1966.In vitro synthesis of brain protein. II. Properties of the complete system. Biochemistry 5:930–936.
Zomzely, C. E., Roberts, S., Peache, S., andBrown, D. M. 1971. Cerebral protein synthesis. J. Biol. Chem. 7:2097–2103.
Yang, J. W., Liu, D. S. H., andRichardson, A. 1977. Biochemical studies of chick brain development and maturation: II. Alterations in the mechanisms of cell-free protein synthesis. Mech. Aging Develop. 6:95–113.
Satake, M., Mase, K., Takahashi, Y., andOgata, K. 1960. Incorporation of leucine into microsomal protein by a cell-free system of guinea pig brain. Biochim. Biophys. Acta 41:366–367.
Dunn, A. J. 1970. The limiting factors of a cell-free protein synthesizing system from rat brain. Biochem. J. 116:135–145.
Barra, H. S., Rodriguez, J. A., Arce, C. A., andCaputto, R. 1973. A soluble preparation from rat brain that incorporates into its own proteins [14C]arginine by a ribonuclease-sensitive and [14C]tyrosine by a ribonuclease-insensitive system. J. Neurochem. 20:97–108.
Lerner, M., andJohnson, T. 1970. Regulation of protein synthesis in developing mouse brain tissue. J. Biol. Chem. 245:1388–1393.
Takahashi, T., andAbe, S. 1963. Distribution of amino acid activating enzymes in rabbit's brain. Experientia 19:186–187.
Pain, V. M., andClemens, M. J. 1973. The role of soluble protein synthesis in eukaryotic cells. FEBS Lett. 32:205–212.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Liu, D.S.H., Yang, J.W. & Richardson, A. Comparison of cell-free protein synthesis by different regions of chicken brain. Neurochem Res 3, 221–238 (1978). https://doi.org/10.1007/BF00964062
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00964062