Heterogeneity of horse spleen ferritin and apoferritin: Comparison of electrophoretic and chromatographic fractions
Horse spleen ferritin and apoferritin each separate into several analogous components in gel electrophoresis. Sedimentation studies indicate that the major components are related as monomer, dimer, and trimer, and that the electrophoretic separation is due to differences in molecular size or shape r...
Gespeichert in:
| Veröffentlicht in: | Archives of biochemistry and biophysics 1965-08, Vol.111 (2), p.399-406 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 406 |
|---|---|
| container_issue | 2 |
| container_start_page | 399 |
| container_title | Archives of biochemistry and biophysics |
| container_volume | 111 |
| creator | Suran, Anita A. Tarver, H. |
| description | Horse spleen ferritin and apoferritin each separate into several analogous components in gel electrophoresis. Sedimentation studies indicate that the major components are related as monomer, dimer, and trimer, and that the electrophoretic separation is due to differences in molecular size or shape rather than to differences in charge. Disulfide bonds do not appear to be involved in the formation of the aggregates. Moreover, the pattern of aggregation could not be altered by various agents which might be expected to disrupt macromolecular aggregates. Chromatography of ferritin on DEAE-cellulose reveals a different and unstable order of heterogeneity, not related to aggregate size. No significant difference in amino acid composition or in “fingerprints” of tryptic peptides of the DEAE fractions could be shown. Fractionation may be due to conformational differences among ferritin molecules. |
| doi_str_mv | 10.1016/0003-9861(65)90202-X |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_85034249</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>000398616590202X</els_id><sourcerecordid>85034249</sourcerecordid><originalsourceid>FETCH-LOGICAL-c357t-5df39627ddbaf1053c33d57380ac6c098ceaec5ebfbb3a8d549c4f0df3699b8b3</originalsourceid><addsrcrecordid>eNp9kMFO3DAQhq2qiC60b9BKOVVwCIzj2BtzQEIrKEhIXKjEzXLsMesqiYPtrcTb42W3HHsazcz_jeWPkO8UzihQcQ4ArJadoCeCn0pooKmfPpEFBSlqYF37mSw-Il_IUUp_AChtRXNIDnknmtItSLrFjDE844Q-v1bBVesQE1ZpHhCnymGMPvup0pOt9Bz-9RfVKoyzjj6FaQvhgCbHMBcYszfvcbOOYdQ5PEc9r8vMRW2yD1P6Sg6cHhJ-29dj8vvm-nF1W98__LpbXd3XhvFlrrl1TIpmaW2vHQXODGOWL1kH2ggDsjOo0XDsXd8z3VneStM6KJSQsu96dkx-7u7OMbxsMGU1-mRwGPSEYZNUx4G1TStLsN0FTQwpRXRqjn7U8VVRUFvXaitSbUUqwdW7a_VUsB_7-5t-RPsB7eWW_eVuj-WTfz1GlYzHyaD1sehSNvj_P_AGInOR1w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>85034249</pqid></control><display><type>article</type><title>Heterogeneity of horse spleen ferritin and apoferritin: Comparison of electrophoretic and chromatographic fractions</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Suran, Anita A. ; Tarver, H.</creator><creatorcontrib>Suran, Anita A. ; Tarver, H.</creatorcontrib><description>Horse spleen ferritin and apoferritin each separate into several analogous components in gel electrophoresis. Sedimentation studies indicate that the major components are related as monomer, dimer, and trimer, and that the electrophoretic separation is due to differences in molecular size or shape rather than to differences in charge. Disulfide bonds do not appear to be involved in the formation of the aggregates. Moreover, the pattern of aggregation could not be altered by various agents which might be expected to disrupt macromolecular aggregates. Chromatography of ferritin on DEAE-cellulose reveals a different and unstable order of heterogeneity, not related to aggregate size. No significant difference in amino acid composition or in “fingerprints” of tryptic peptides of the DEAE fractions could be shown. Fractionation may be due to conformational differences among ferritin molecules.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(65)90202-X</identifier><identifier>PMID: 5862001</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acids ; Animals ; Cellulose ; Chemical Phenomena ; Chemistry ; Chemistry Techniques, Analytical ; Chromatography ; Electrophoresis ; Ferritins ; Horses ; In Vitro Techniques ; Spleen ; Ultracentrifugation</subject><ispartof>Archives of biochemistry and biophysics, 1965-08, Vol.111 (2), p.399-406</ispartof><rights>1965</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-5df39627ddbaf1053c33d57380ac6c098ceaec5ebfbb3a8d549c4f0df3699b8b3</citedby><cites>FETCH-LOGICAL-c357t-5df39627ddbaf1053c33d57380ac6c098ceaec5ebfbb3a8d549c4f0df3699b8b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/000398616590202X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/5862001$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Suran, Anita A.</creatorcontrib><creatorcontrib>Tarver, H.</creatorcontrib><title>Heterogeneity of horse spleen ferritin and apoferritin: Comparison of electrophoretic and chromatographic fractions</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Horse spleen ferritin and apoferritin each separate into several analogous components in gel electrophoresis. Sedimentation studies indicate that the major components are related as monomer, dimer, and trimer, and that the electrophoretic separation is due to differences in molecular size or shape rather than to differences in charge. Disulfide bonds do not appear to be involved in the formation of the aggregates. Moreover, the pattern of aggregation could not be altered by various agents which might be expected to disrupt macromolecular aggregates. Chromatography of ferritin on DEAE-cellulose reveals a different and unstable order of heterogeneity, not related to aggregate size. No significant difference in amino acid composition or in “fingerprints” of tryptic peptides of the DEAE fractions could be shown. Fractionation may be due to conformational differences among ferritin molecules.</description><subject>Amino Acids</subject><subject>Animals</subject><subject>Cellulose</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Chemistry Techniques, Analytical</subject><subject>Chromatography</subject><subject>Electrophoresis</subject><subject>Ferritins</subject><subject>Horses</subject><subject>In Vitro Techniques</subject><subject>Spleen</subject><subject>Ultracentrifugation</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1965</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMFO3DAQhq2qiC60b9BKOVVwCIzj2BtzQEIrKEhIXKjEzXLsMesqiYPtrcTb42W3HHsazcz_jeWPkO8UzihQcQ4ArJadoCeCn0pooKmfPpEFBSlqYF37mSw-Il_IUUp_AChtRXNIDnknmtItSLrFjDE844Q-v1bBVesQE1ZpHhCnymGMPvup0pOt9Bz-9RfVKoyzjj6FaQvhgCbHMBcYszfvcbOOYdQ5PEc9r8vMRW2yD1P6Sg6cHhJ-29dj8vvm-nF1W98__LpbXd3XhvFlrrl1TIpmaW2vHQXODGOWL1kH2ggDsjOo0XDsXd8z3VneStM6KJSQsu96dkx-7u7OMbxsMGU1-mRwGPSEYZNUx4G1TStLsN0FTQwpRXRqjn7U8VVRUFvXaitSbUUqwdW7a_VUsB_7-5t-RPsB7eWW_eVuj-WTfz1GlYzHyaD1sehSNvj_P_AGInOR1w</recordid><startdate>196508</startdate><enddate>196508</enddate><creator>Suran, Anita A.</creator><creator>Tarver, H.</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>196508</creationdate><title>Heterogeneity of horse spleen ferritin and apoferritin: Comparison of electrophoretic and chromatographic fractions</title><author>Suran, Anita A. ; Tarver, H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-5df39627ddbaf1053c33d57380ac6c098ceaec5ebfbb3a8d549c4f0df3699b8b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1965</creationdate><topic>Amino Acids</topic><topic>Animals</topic><topic>Cellulose</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Chemistry Techniques, Analytical</topic><topic>Chromatography</topic><topic>Electrophoresis</topic><topic>Ferritins</topic><topic>Horses</topic><topic>In Vitro Techniques</topic><topic>Spleen</topic><topic>Ultracentrifugation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Suran, Anita A.</creatorcontrib><creatorcontrib>Tarver, H.</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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Suran, Anita A.</au><au>Tarver, H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heterogeneity of horse spleen ferritin and apoferritin: Comparison of electrophoretic and chromatographic fractions</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1965-08</date><risdate>1965</risdate><volume>111</volume><issue>2</issue><spage>399</spage><epage>406</epage><pages>399-406</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>Horse spleen ferritin and apoferritin each separate into several analogous components in gel electrophoresis. Sedimentation studies indicate that the major components are related as monomer, dimer, and trimer, and that the electrophoretic separation is due to differences in molecular size or shape rather than to differences in charge. Disulfide bonds do not appear to be involved in the formation of the aggregates. Moreover, the pattern of aggregation could not be altered by various agents which might be expected to disrupt macromolecular aggregates. Chromatography of ferritin on DEAE-cellulose reveals a different and unstable order of heterogeneity, not related to aggregate size. No significant difference in amino acid composition or in “fingerprints” of tryptic peptides of the DEAE fractions could be shown. Fractionation may be due to conformational differences among ferritin molecules.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>5862001</pmid><doi>10.1016/0003-9861(65)90202-X</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1965-08, Vol.111 (2), p.399-406 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_85034249 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acids Animals Cellulose Chemical Phenomena Chemistry Chemistry Techniques, Analytical Chromatography Electrophoresis Ferritins Horses In Vitro Techniques Spleen Ultracentrifugation |
| title | Heterogeneity of horse spleen ferritin and apoferritin: Comparison of electrophoretic and chromatographic fractions |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-31T02%3A50%3A47IST&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=Heterogeneity%20of%20horse%20spleen%20ferritin%20and%20apoferritin:%20Comparison%20of%20electrophoretic%20and%20chromatographic%20fractions&rft.jtitle=Archives%20of%20biochemistry%20and%20biophysics&rft.au=Suran,%20Anita%20A.&rft.date=1965-08&rft.volume=111&rft.issue=2&rft.spage=399&rft.epage=406&rft.pages=399-406&rft.issn=0003-9861&rft.eissn=1096-0384&rft_id=info:doi/10.1016/0003-9861(65)90202-X&rft_dat=%3Cproquest_cross%3E85034249%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=85034249&rft_id=info:pmid/5862001&rft_els_id=000398616590202X&rfr_iscdi=true |