Occurrence of a methylated protein in chloroplast ribosomes
A ribosomal protein of spinach chloroplast, previously shown to be immunologically homologous to Escherichia coli ribosomal protein L2, was purified by using gel filtration, ion-exchange chromatography, and reverse-phase high-performance liquid chromatography separation. Methyl modification of prote...
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Published in | Biochemistry (Easton) Vol. 26; no. 18; pp. 5866 - 5870 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Chemical Society
08.09.1987
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Subjects | |
Online Access | Get full text |
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Summary: | A ribosomal protein of spinach chloroplast, previously shown to be immunologically homologous to Escherichia coli ribosomal protein L2, was purified by using gel filtration, ion-exchange chromatography, and reverse-phase high-performance liquid chromatography separation. Methyl modification of proteins, whose occurrence in E. coli ribosomes is established, is present in chloroplast ribosomes as well. This and the additional significance of the amino acid sequence data reported in this paper are discussed. |
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Bibliography: | F60 880265488 ark:/67375/TPS-QFBXR1DM-D istex:50F1912EEDFC9717E28CE9614E43321FA7481F8C ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
ISSN: | 0006-2960 1520-4995 |
DOI: | 10.1021/bi00392a043 |