Structural polypeptides of three rhinoviruses
Growth, purification and electrophoretic analysis of three rhinoviruses and an enterovirus are described. It is shown that, with regard to structural polypeptides, the three rhinoviruses differ from other picornaviruses, and from each other. However, all three rhinoviruses resemble one another in po...
Gespeichert in:
Veröffentlicht in: | Biochemical and biophysical research communications 1970-10, Vol.41 (2), p.477-481 |
---|---|
Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 481 |
---|---|
container_issue | 2 |
container_start_page | 477 |
container_title | Biochemical and biophysical research communications |
container_volume | 41 |
creator | Korant, B.D. Lonberg-Holm, K.K. Halperen, S. |
description | Growth, purification and electrophoretic analysis of three rhinoviruses and an enterovirus are described. It is shown that, with regard to structural polypeptides, the three rhinoviruses differ from other picornaviruses, and from each other. However, all three rhinoviruses resemble one another in possessing structural polypeptides of molecular weights 33,000 and 30,000 in similar proportions. |
doi_str_mv | 10.1016/0006-291X(70)90530-9 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80829762</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0006291X70905309</els_id><sourcerecordid>80829762</sourcerecordid><originalsourceid>FETCH-LOGICAL-c272t-836e13d3eb077194b607142c39bbbb89cca755c2235cf2631e7f81c5be868ce33</originalsourceid><addsrcrecordid>eNp9kM9LwzAUx4Moc07_A4WeRA_Rl6RNmoswhr9g4EEFb6FNX1mkW2rSDvbf27mxo-_yDt8fj_ch5JLBHQMm7wFAUq7Z142CWw2ZAKqPyJiBBsoZpMdkfLCckrMYvwEYS6UekVEqeCaVGBP63oXedn0omqT1zabFtnMVxsTXSbcIiElYuJVfu9BHjOfkpC6aiBf7PSGfT48fsxc6f3t-nU3n1HLFO5oLiUxUAktQium0lKBYyq3Q5TC5trZQWWY5F5mtuRQMVZ0zm5WYy9yiEBNyvettg__pMXZm6aLFpilW6Ptocsi5VpIPxnRntMHHGLA2bXDLImwMA7OlZLYIzBaBUWD-KBk9xK72_X25xOoQ2mMZ9IedjsOTa4fBROtwZbFyAW1nKu_-P_ALG3t2Ig</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>80829762</pqid></control><display><type>article</type><title>Structural polypeptides of three rhinoviruses</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Korant, B.D. ; Lonberg-Holm, K.K. ; Halperen, S.</creator><creatorcontrib>Korant, B.D. ; Lonberg-Holm, K.K. ; Halperen, S.</creatorcontrib><description>Growth, purification and electrophoretic analysis of three rhinoviruses and an enterovirus are described. It is shown that, with regard to structural polypeptides, the three rhinoviruses differ from other picornaviruses, and from each other. However, all three rhinoviruses resemble one another in possessing structural polypeptides of molecular weights 33,000 and 30,000 in similar proportions.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(70)90530-9</identifier><identifier>PMID: 4325673</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acids ; Animals ; Carbon Isotopes ; Centrifugation, Density Gradient ; Chemical Phenomena ; Chemistry ; Electrophoresis ; Enterovirus - analysis ; Enterovirus - metabolism ; HeLa Cells ; Horses ; Hydrogen-Ion Concentration ; Kidney ; Macaca ; Molecular Weight ; Peptides - analysis ; Rhinovirus - analysis ; Rhinovirus - isolation & purification ; Species Specificity ; Virus Cultivation</subject><ispartof>Biochemical and biophysical research communications, 1970-10, Vol.41 (2), p.477-481</ispartof><rights>1970</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c272t-836e13d3eb077194b607142c39bbbb89cca755c2235cf2631e7f81c5be868ce33</citedby><cites>FETCH-LOGICAL-c272t-836e13d3eb077194b607142c39bbbb89cca755c2235cf2631e7f81c5be868ce33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006291X70905309$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4325673$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Korant, B.D.</creatorcontrib><creatorcontrib>Lonberg-Holm, K.K.</creatorcontrib><creatorcontrib>Halperen, S.</creatorcontrib><title>Structural polypeptides of three rhinoviruses</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Growth, purification and electrophoretic analysis of three rhinoviruses and an enterovirus are described. It is shown that, with regard to structural polypeptides, the three rhinoviruses differ from other picornaviruses, and from each other. However, all three rhinoviruses resemble one another in possessing structural polypeptides of molecular weights 33,000 and 30,000 in similar proportions.</description><subject>Amino Acids</subject><subject>Animals</subject><subject>Carbon Isotopes</subject><subject>Centrifugation, Density Gradient</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Electrophoresis</subject><subject>Enterovirus - analysis</subject><subject>Enterovirus - metabolism</subject><subject>HeLa Cells</subject><subject>Horses</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kidney</subject><subject>Macaca</subject><subject>Molecular Weight</subject><subject>Peptides - analysis</subject><subject>Rhinovirus - analysis</subject><subject>Rhinovirus - isolation & purification</subject><subject>Species Specificity</subject><subject>Virus Cultivation</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1970</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM9LwzAUx4Moc07_A4WeRA_Rl6RNmoswhr9g4EEFb6FNX1mkW2rSDvbf27mxo-_yDt8fj_ch5JLBHQMm7wFAUq7Z142CWw2ZAKqPyJiBBsoZpMdkfLCckrMYvwEYS6UekVEqeCaVGBP63oXedn0omqT1zabFtnMVxsTXSbcIiElYuJVfu9BHjOfkpC6aiBf7PSGfT48fsxc6f3t-nU3n1HLFO5oLiUxUAktQium0lKBYyq3Q5TC5trZQWWY5F5mtuRQMVZ0zm5WYy9yiEBNyvettg__pMXZm6aLFpilW6Ptocsi5VpIPxnRntMHHGLA2bXDLImwMA7OlZLYIzBaBUWD-KBk9xK72_X25xOoQ2mMZ9IedjsOTa4fBROtwZbFyAW1nKu_-P_ALG3t2Ig</recordid><startdate>19701023</startdate><enddate>19701023</enddate><creator>Korant, B.D.</creator><creator>Lonberg-Holm, K.K.</creator><creator>Halperen, S.</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19701023</creationdate><title>Structural polypeptides of three rhinoviruses</title><author>Korant, B.D. ; Lonberg-Holm, K.K. ; Halperen, S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c272t-836e13d3eb077194b607142c39bbbb89cca755c2235cf2631e7f81c5be868ce33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1970</creationdate><topic>Amino Acids</topic><topic>Animals</topic><topic>Carbon Isotopes</topic><topic>Centrifugation, Density Gradient</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Electrophoresis</topic><topic>Enterovirus - analysis</topic><topic>Enterovirus - metabolism</topic><topic>HeLa Cells</topic><topic>Horses</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kidney</topic><topic>Macaca</topic><topic>Molecular Weight</topic><topic>Peptides - analysis</topic><topic>Rhinovirus - analysis</topic><topic>Rhinovirus - isolation & purification</topic><topic>Species Specificity</topic><topic>Virus Cultivation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Korant, B.D.</creatorcontrib><creatorcontrib>Lonberg-Holm, K.K.</creatorcontrib><creatorcontrib>Halperen, S.</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><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Korant, B.D.</au><au>Lonberg-Holm, K.K.</au><au>Halperen, S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural polypeptides of three rhinoviruses</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1970-10-23</date><risdate>1970</risdate><volume>41</volume><issue>2</issue><spage>477</spage><epage>481</epage><pages>477-481</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Growth, purification and electrophoretic analysis of three rhinoviruses and an enterovirus are described. It is shown that, with regard to structural polypeptides, the three rhinoviruses differ from other picornaviruses, and from each other. However, all three rhinoviruses resemble one another in possessing structural polypeptides of molecular weights 33,000 and 30,000 in similar proportions.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4325673</pmid><doi>10.1016/0006-291X(70)90530-9</doi><tpages>5</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0006-291X |
ispartof | Biochemical and biophysical research communications, 1970-10, Vol.41 (2), p.477-481 |
issn | 0006-291X 1090-2104 |
language | eng |
recordid | cdi_proquest_miscellaneous_80829762 |
source | MEDLINE; Elsevier ScienceDirect Journals |
subjects | Amino Acids Animals Carbon Isotopes Centrifugation, Density Gradient Chemical Phenomena Chemistry Electrophoresis Enterovirus - analysis Enterovirus - metabolism HeLa Cells Horses Hydrogen-Ion Concentration Kidney Macaca Molecular Weight Peptides - analysis Rhinovirus - analysis Rhinovirus - isolation & purification Species Specificity Virus Cultivation |
title | Structural polypeptides of three rhinoviruses |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-03T00%3A43%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structural%20polypeptides%20of%20three%20rhinoviruses&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Korant,%20B.D.&rft.date=1970-10-23&rft.volume=41&rft.issue=2&rft.spage=477&rft.epage=481&rft.pages=477-481&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/0006-291X(70)90530-9&rft_dat=%3Cproquest_cross%3E80829762%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=80829762&rft_id=info:pmid/4325673&rft_els_id=0006291X70905309&rfr_iscdi=true |