Summary
Ribosomes were isolated from normal and growing kidney and the protein complement was examined by a two-dimensional gel electrophoretic procedure. Proteins were resolved in the first dimension on the basis of charge and, in the second dimension, on the basis of molecular weight. 60S and 40S ribosomal subunits from normal kidney contained respectively 42 and 31 proteins. 80S ribosomes contained 23 proteins not found with either sub-unit. Nineteen of these proteins were removed from the ribosomes when isolated ribosomes were washed in a high salt buffer. Six proteins of the 80S ribosome corresponded to proteins associated with both sub-units. 80S ribosomal proteins were also studied during compensatory renal hypertrophy after 4-96 h of induced growth. The protein complement displayed by electrophoresis was identical to the pattern seen from normal renal cells.
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Abbreviations
- Bis-Tris:
-
[bis(2-Hydroxyethyl)imino-tris (Hydroxymethyl)methane]
- MES:
-
2(N-morpholino)ethane sulfonic acid
References
Bucher, N. L. R. and Malt, R. A., 1971. Regeneration of Liver and Kidney, Little, Brown and Co, Boston.
Melvin, W. T., Kumar, A. and Malt, R. A., 1976. J. Cell Biol. 69, 548–556.
Hill, J. M. and Malamud, D., 1974. FEBS Letters 46, 308–310.
Hill, J. M., 1976. Personal Communication.
Sendecki, W., Kuliszewski, M. and Patzer, J., 1973. Acta Biochim. Polonica 20, 63–71.
Hardy, S. J. S., Kurland, C. G., Voynow, P. and Mora, G., 1969. Biochemistry 8, 2897–2905.
Mets, L. and Bogorad, L., 1974. Anal. Biochem. 57, 200–210.
Weber, K., Pringle, J. R. and Osborn, M., 1972. Methods in Enzymology, Part C 26, 3–27.
Sherton, C. C. and Wool, I. G., 1974. J. Biol. Chem. 249, 2258–2266.
Delannay, J., Matheiu, C. and Schapira, G., 1972. Eur. J. Biochem. 31, 561–564.
Martini, O. H. W. and Gould, H. J., 1971. J. Mol. Biol. 62, 403–405.
Gressner, A. M. and Wool. I. G. (1974) J. Biol. Chem. 249, 6917–6925.
Kaltschmidt, E. and Wittmann, H. G., 1970. Anal. Biochem. 36, 401–412.
Subramanian, A. R., 1974. Eur. J. Biochem. 45, 541–546.
Sherton, C. C. and Wool. I. G. 1974. Methods in Enzymology, Part F 30, 506–526.
Rodgers, A., 1973. Biochim. Biophys. Acta. 294, 292–296.
Anderson, W. M., Grundholm, A. and Sells, B. H., 1975. Biochem. Biophys. Res. Commun. 62, 669–676.
Kuliszewski, M., Szumilo, M., Rahden, I. and Sendecki, W., 1976. Acta Biochim. Polonica 23, 27–36.
Subramanian, A. R., Gilbert, J. M. and Kumar, A., 1975. Biochim. Biophys. Acta. 383, 94–96. AMINOACYL-tRNA SYNTHETASES FROM CALE LIVER: OPTIMIZED ASSAY CONDITIONS AND KINETIC PROPERTIES Alfred H. F. CHOO and David M. LOGAN Department of Biology, York University, Downsview, Ontario, Canada (Received January 17, 1977)
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Supported by NIH Grants AM-12769 and RR-05486 and the Damon Runyon-Walter Winchell Fund. Dr. Irwin is a fellow of the Damon Runyon-Walter Winchell Fund (DRG-51-F). Dr.Northrup is a Research Fellow in Developmental Medicine (HD00362) at Massachusetts General Hospital.
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Northrup, T.E., Irwin, D. & Malt, R.A. Ribosomal proteins of mouse kidney: Normal status and during compensatory renal hypertrophy. Mol Cell Biochem 17, 25–30 (1977). https://doi.org/10.1007/BF01732551
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DOI: https://doi.org/10.1007/BF01732551