{"title":"Fractionation studies of the ribosomal proteins from Escherichia coli","authors":"Wim Möller, Jean Widdowson","doi":"10.1016/0022-2836(67)90224-0","DOIUrl":null,"url":null,"abstract":"<div><div>Ribosomal proteins from <em>Escherichia coli</em> were fractionated by column chromatography on carboxymethyl-cellulose, using 8 <span>m</span>-urea solutions (pH 8.0) and a salt gradient. The resulting fractions were characterized by disc electrophoresis in polyacrylamide gels and by determination of amino acid composition and tryptic peptide distribution. Ribosomal proteins were fractionated into four classes of chemically different proteins. All but one class appeared to be complex and composed of multiple proteins by every criterion employed. An acidic protein, called ribosomal A protein, was isolated and partially characterized. On the average, each 70 s ribosome is estimated to contain two to three molecules of this protein. The chemical heterogeneity of ribosomal proteins was found to be large. Variability in amino acid sequence within a limited number of different classes of ribosomal proteins may contribute to the over-all complexity of these proteins.</div></div>","PeriodicalId":369,"journal":{"name":"Journal of Molecular Biology","volume":"24 3","pages":"Pages 367-370, IN1-IN3, 371-378"},"PeriodicalIF":4.5000,"publicationDate":"1967-03-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Molecular Biology","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0022283667902240","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Ribosomal proteins from Escherichia coli were fractionated by column chromatography on carboxymethyl-cellulose, using 8 m-urea solutions (pH 8.0) and a salt gradient. The resulting fractions were characterized by disc electrophoresis in polyacrylamide gels and by determination of amino acid composition and tryptic peptide distribution. Ribosomal proteins were fractionated into four classes of chemically different proteins. All but one class appeared to be complex and composed of multiple proteins by every criterion employed. An acidic protein, called ribosomal A protein, was isolated and partially characterized. On the average, each 70 s ribosome is estimated to contain two to three molecules of this protein. The chemical heterogeneity of ribosomal proteins was found to be large. Variability in amino acid sequence within a limited number of different classes of ribosomal proteins may contribute to the over-all complexity of these proteins.
期刊介绍：
Journal of Molecular Biology (JMB) provides high quality, comprehensive and broad coverage in all areas of molecular biology. The journal publishes original scientific research papers that provide mechanistic and functional insights and report a significant advance to the field. The journal encourages the submission of multidisciplinary studies that use complementary experimental and computational approaches to address challenging biological questions.
Research areas include but are not limited to: Biomolecular interactions, signaling networks, systems biology; Cell cycle, cell growth, cell differentiation; Cell death, autophagy; Cell signaling and regulation; Chemical biology; Computational biology, in combination with experimental studies; DNA replication, repair, and recombination; Development, regenerative biology, mechanistic and functional studies of stem cells; Epigenetics, chromatin structure and function; Gene expression; Membrane processes, cell surface proteins and cell-cell interactions; Methodological advances, both experimental and theoretical, including databases; Microbiology, virology, and interactions with the host or environment; Microbiota mechanistic and functional studies; Nuclear organization; Post-translational modifications, proteomics; Processing and function of biologically important macromolecules and complexes; Molecular basis of disease; RNA processing, structure and functions of non-coding RNAs, transcription; Sorting, spatiotemporal organization, trafficking; Structural biology; Synthetic biology; Translation, protein folding, chaperones, protein degradation and quality control.
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