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Isolation and Characterization of Two Acidic Proteins of 60S Ribosomes from Artemia salina Cysts
60S ribosomes from encysted gastrulae of the brine shrimp Artemia salina contain two acidic proteins, which are homologous to the Escherichia coli proteins L7 and L12. The proteins were purified and characterized with respect to molecular weight, amino-acid composition, peptide maps, and their funct...
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Published in: | Proceedings of the National Academy of Sciences - PNAS 1975-12, Vol.72 (12), p.4744-4748 |
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container_issue | 12 |
container_start_page | 4744 |
container_title | Proceedings of the National Academy of Sciences - PNAS |
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creator | Moller, W. Slobin, L. I. Amons, R. Richter, D. |
description | 60S ribosomes from encysted gastrulae of the brine shrimp Artemia salina contain two acidic proteins, which are homologous to the Escherichia coli proteins L7 and L12. The proteins were purified and characterized with respect to molecular weight, amino-acid composition, peptide maps, and their functional requirement in the elongation factor dependent binding of aminoacyl transfer RNA to the ribosome. |
doi_str_mv | 10.1073/pnas.72.12.4744 |
format | article |
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The proteins were purified and characterized with respect to molecular weight, amino-acid composition, peptide maps, and their functional requirement in the elongation factor dependent binding of aminoacyl transfer RNA to the ribosome.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.72.12.4744</identifier><identifier>PMID: 1061068</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amino Acids - analysis ; Animals ; Artemia ; Binding Sites ; Biochemistry ; Cysts ; Decapoda (Crustacea) ; Electrophoresis ; Gels ; Molecular Weight ; Peptide Chain Elongation, Translational ; Peptide Elongation Factors ; Peptide Fragments - analysis ; Protein Binding ; Ribosomal proteins ; Ribosomal Proteins - analysis ; Ribosomes ; Ribosomes - chemistry ; Ribosomes - metabolism ; RNA, Transfer - metabolism ; Sodium ; Sulfates ; Transfer RNA</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1975-12, Vol.72 (12), p.4744-4748</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3764-5661533eafbd5a05eb6068f91add84a4744f506656759ee1cd440f22463df46d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/72/12.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/65279$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/65279$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793,58238,58471</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1061068$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Moller, W.</creatorcontrib><creatorcontrib>Slobin, L. 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I. ; Amons, R. ; Richter, D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3764-5661533eafbd5a05eb6068f91add84a4744f506656759ee1cd440f22463df46d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Artemia</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Cysts</topic><topic>Decapoda (Crustacea)</topic><topic>Electrophoresis</topic><topic>Gels</topic><topic>Molecular Weight</topic><topic>Peptide Chain Elongation, Translational</topic><topic>Peptide Elongation Factors</topic><topic>Peptide Fragments - analysis</topic><topic>Protein Binding</topic><topic>Ribosomal proteins</topic><topic>Ribosomal Proteins - analysis</topic><topic>Ribosomes</topic><topic>Ribosomes - chemistry</topic><topic>Ribosomes - metabolism</topic><topic>RNA, Transfer - metabolism</topic><topic>Sodium</topic><topic>Sulfates</topic><topic>Transfer RNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Moller, W.</creatorcontrib><creatorcontrib>Slobin, L. I.</creatorcontrib><creatorcontrib>Amons, R.</creatorcontrib><creatorcontrib>Richter, D.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Moller, W.</au><au>Slobin, L. I.</au><au>Amons, R.</au><au>Richter, D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and Characterization of Two Acidic Proteins of 60S Ribosomes from Artemia salina Cysts</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1975-12-01</date><risdate>1975</risdate><volume>72</volume><issue>12</issue><spage>4744</spage><epage>4748</epage><pages>4744-4748</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>60S ribosomes from encysted gastrulae of the brine shrimp Artemia salina contain two acidic proteins, which are homologous to the Escherichia coli proteins L7 and L12. The proteins were purified and characterized with respect to molecular weight, amino-acid composition, peptide maps, and their functional requirement in the elongation factor dependent binding of aminoacyl transfer RNA to the ribosome.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>1061068</pmid><doi>10.1073/pnas.72.12.4744</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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identifier | ISSN: 0027-8424 |
ispartof | Proceedings of the National Academy of Sciences - PNAS, 1975-12, Vol.72 (12), p.4744-4748 |
issn | 0027-8424 1091-6490 |
language | eng |
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source | JSTOR Archival Journals and Primary Sources Collection; PubMed Central |
subjects | Amino Acids - analysis Animals Artemia Binding Sites Biochemistry Cysts Decapoda (Crustacea) Electrophoresis Gels Molecular Weight Peptide Chain Elongation, Translational Peptide Elongation Factors Peptide Fragments - analysis Protein Binding Ribosomal proteins Ribosomal Proteins - analysis Ribosomes Ribosomes - chemistry Ribosomes - metabolism RNA, Transfer - metabolism Sodium Sulfates Transfer RNA |
title | Isolation and Characterization of Two Acidic Proteins of 60S Ribosomes from Artemia salina Cysts |
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