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Current Genetics, 1987
Using a heterologous probe containing a fragment of the L25-gene from Saccharomyces carlsbergensis we have isolated a DNA-fragment of Candida utilis carrying the gene encoding ribosomal protein L25. This gene is present in a single copy on the C. utilis genome, though as two distinguishable alleles.
L P, Woudt +4 more
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Using a heterologous probe containing a fragment of the L25-gene from Saccharomyces carlsbergensis we have isolated a DNA-fragment of Candida utilis carrying the gene encoding ribosomal protein L25. This gene is present in a single copy on the C. utilis genome, though as two distinguishable alleles.
L P, Woudt +4 more
exaly +3 more sources
The Primary Structure of the 5S rRNA Binding Protein L25 of Escherichia coli Ribosomes
Hoppe-Seyler's Zeitschrift Für Physiologische Chemie, 1975The primary structure of protein L25 from the large subunit of Escherichia coli ribosomes was determined by isolation and analysis of peptides obtained after cleavage of the protein with trypsin, thermolysin and Staphylococcus protease as well as by Edman degradation of the intact protein and of a CNBr peptide. The complete amino acid sequence is shown
K G, Bitar, B, Wittmann-Liebold
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Journal of Molecular Biology, 1991
The regions of the large subunit ribosomal protein L25 from Saccharomyces cerevisiae responsible for nuclear localization of the protein were identified by constructing fusion genes encoding various segments of L25 linked to the amino terminus of beta-galactosidase.
Peter J Schaap
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The regions of the large subunit ribosomal protein L25 from Saccharomyces cerevisiae responsible for nuclear localization of the protein were identified by constructing fusion genes encoding various segments of L25 linked to the amino terminus of beta-galactosidase.
Peter J Schaap
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Biochimica Et Biophysica Acta Gene Regulatory Mechanisms, 1990
We have developed a combination of in vivo and in vitro methods which allows us to determine the effect of practically every structural change, deletions as well as point mutations, on various biological functions of a ribosomal protein (r-protein).
C A, Rutgers +4 more
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We have developed a combination of in vivo and in vitro methods which allows us to determine the effect of practically every structural change, deletions as well as point mutations, on various biological functions of a ribosomal protein (r-protein).
C A, Rutgers +4 more
exaly +3 more sources
rRNA binding domain of yeast ribosomal protein L25
Journal of Molecular Biology, 1991Carla A. Rutgers +3 more
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2023
The Minor Planet Electronic Circulars contain information on unusual minor planets, routine data on comets and natural satellites, and occasional editorial announcements. They are published on behalf of Division F of the International Astronomical Union by the Minor Planet Center, Smithsonian Astrophysical Observatory, Cambridge, MA 02138, U.S.A.
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The Minor Planet Electronic Circulars contain information on unusual minor planets, routine data on comets and natural satellites, and occasional editorial announcements. They are published on behalf of Division F of the International Astronomical Union by the Minor Planet Center, Smithsonian Astrophysical Observatory, Cambridge, MA 02138, U.S.A.
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Thyroid uptake measurement using iodine-l25 and iodine-l31
Physics in Medicine & Biology, 1969Due to the low energy (27.4 kev) of the photons emitted by 125I, the external measurement of thyroid activity requires a significant correction for tissue absorption. This correction can be determined by administering simultaneously a low dose of 131I.
null P Espinasse +2 more
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Purification and conformation of ribosomal protein L25 from E. coli ribosome
International Journal of Peptide and Protein Research, 1988Ribosomal protein L25 from the large subunit of E. coli ribosomes has been purified using a new procedure involving a 2 m LiCl extraction followed by phosphocellulose chromatography in 6 m urea elution buffer. The conformation of purified L25 was studied employing circular dichroism and ultraviolet absorption spectroscopy in reconstitution buffer.
J W, Fox, D P, Owens, K P, Wong
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