Postsecretory modifications of streptavidin
Streptavidin, an extracellular biotin-binding protein from Streptomyces avidinii, exhibits a multiplicity in its electrophoretic mobility pattern which depends both upon the conditions for growth of the bacterium and upon the protocol used in the purification of the protein. The observed structural...
Gespeichert in:
| Veröffentlicht in: | Biochemical journal 1989-04, Vol.259 (2), p.369-376 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 376 |
|---|---|
| container_issue | 2 |
| container_start_page | 369 |
| container_title | Biochemical journal |
| container_volume | 259 |
| creator | Bayer, E A Ben-Hur, H Hiller, Y Wilchek, M |
| description | Streptavidin, an extracellular biotin-binding protein from Streptomyces avidinii, exhibits a multiplicity in its electrophoretic mobility pattern which depends both upon the conditions for growth of the bacterium and upon the protocol used in the purification of the protein. The observed structural heterogeneity appears to reflect the action of two types of postsecretory molecular events: proteolytic digestion of the intact Mr-18,000 subunit to a minimal molecular size (approx. Mr 14,000), and aggregation of the native tetramer into higher-order oligomeric forms. The extent of subunit degradation and/or tetrameric aggregation affects the capacity of a given streptavidin preparation to interact with biotin-conjugated proteins in different assay systems. |
| doi_str_mv | 10.1042/bj2590369 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1138520</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>78972855</sourcerecordid><originalsourceid>FETCH-LOGICAL-c467t-72da6796fbee18af33c2ef2597c1b20e136c7560e95061280555f7f274d73dde3</originalsourceid><addsrcrecordid>eNqFkUtLAzEUhYMotVYX_gChK0FkNO_MbAQpvqCgC12HTOZGIzOTmqSF_ntHWoquXN3F_fg4nIPQKcFXBHN6XX9SUWEmqz00JlzholS03EdjTCUvJKbkEB2l9Ikx4ZjjERpRRSop-BhdvoSUE9gIOcT1tAuNd96a7EOfpsFNU46wyGblG98fowNn2gQn2ztBb_d3r7PHYv788DS7nReWS5ULRRsjVSVdDUBK4xizFNwQUFlSUwyESauExFAJLAktsRDCKUcVbxRrGmATdLPxLpZ1B42FPkfT6kX0nYlrHYzXfz-9_9DvYaUJYaWgeBCcbwUxfC0hZd35ZKFtTQ9hmbQqq6EfIf4FiWCUsZIO4MUGtDGkFMHt0hCsfybQuwkG9ux3_B257Zx9A_TLgXU</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15323382</pqid></control><display><type>article</type><title>Postsecretory modifications of streptavidin</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><creator>Bayer, E A ; Ben-Hur, H ; Hiller, Y ; Wilchek, M</creator><creatorcontrib>Bayer, E A ; Ben-Hur, H ; Hiller, Y ; Wilchek, M</creatorcontrib><description>Streptavidin, an extracellular biotin-binding protein from Streptomyces avidinii, exhibits a multiplicity in its electrophoretic mobility pattern which depends both upon the conditions for growth of the bacterium and upon the protocol used in the purification of the protein. The observed structural heterogeneity appears to reflect the action of two types of postsecretory molecular events: proteolytic digestion of the intact Mr-18,000 subunit to a minimal molecular size (approx. Mr 14,000), and aggregation of the native tetramer into higher-order oligomeric forms. The extent of subunit degradation and/or tetrameric aggregation affects the capacity of a given streptavidin preparation to interact with biotin-conjugated proteins in different assay systems.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj2590369</identifier><identifier>PMID: 2719654</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Bacterial Proteins - isolation & purification ; Bacterial Proteins - metabolism ; Biotin - metabolism ; biotin-binding protein ; Electrophoresis, Polyacrylamide Gel ; Molecular Sequence Data ; Molecular Weight ; Protein Conformation ; Streptavidin</subject><ispartof>Biochemical journal, 1989-04, Vol.259 (2), p.369-376</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c467t-72da6796fbee18af33c2ef2597c1b20e136c7560e95061280555f7f274d73dde3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1138520/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1138520/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2719654$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bayer, E A</creatorcontrib><creatorcontrib>Ben-Hur, H</creatorcontrib><creatorcontrib>Hiller, Y</creatorcontrib><creatorcontrib>Wilchek, M</creatorcontrib><title>Postsecretory modifications of streptavidin</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>Streptavidin, an extracellular biotin-binding protein from Streptomyces avidinii, exhibits a multiplicity in its electrophoretic mobility pattern which depends both upon the conditions for growth of the bacterium and upon the protocol used in the purification of the protein. The observed structural heterogeneity appears to reflect the action of two types of postsecretory molecular events: proteolytic digestion of the intact Mr-18,000 subunit to a minimal molecular size (approx. Mr 14,000), and aggregation of the native tetramer into higher-order oligomeric forms. The extent of subunit degradation and/or tetrameric aggregation affects the capacity of a given streptavidin preparation to interact with biotin-conjugated proteins in different assay systems.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biotin - metabolism</subject><subject>biotin-binding protein</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Protein Conformation</subject><subject>Streptavidin</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtLAzEUhYMotVYX_gChK0FkNO_MbAQpvqCgC12HTOZGIzOTmqSF_ntHWoquXN3F_fg4nIPQKcFXBHN6XX9SUWEmqz00JlzholS03EdjTCUvJKbkEB2l9Ikx4ZjjERpRRSop-BhdvoSUE9gIOcT1tAuNd96a7EOfpsFNU46wyGblG98fowNn2gQn2ztBb_d3r7PHYv788DS7nReWS5ULRRsjVSVdDUBK4xizFNwQUFlSUwyESauExFAJLAktsRDCKUcVbxRrGmATdLPxLpZ1B42FPkfT6kX0nYlrHYzXfz-9_9DvYaUJYaWgeBCcbwUxfC0hZd35ZKFtTQ9hmbQqq6EfIf4FiWCUsZIO4MUGtDGkFMHt0hCsfybQuwkG9ux3_B257Zx9A_TLgXU</recordid><startdate>19890415</startdate><enddate>19890415</enddate><creator>Bayer, E A</creator><creator>Ben-Hur, H</creator><creator>Hiller, Y</creator><creator>Wilchek, M</creator><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19890415</creationdate><title>Postsecretory modifications of streptavidin</title><author>Bayer, E A ; Ben-Hur, H ; Hiller, Y ; Wilchek, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c467t-72da6796fbee18af33c2ef2597c1b20e136c7560e95061280555f7f274d73dde3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biotin - metabolism</topic><topic>biotin-binding protein</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Protein Conformation</topic><topic>Streptavidin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bayer, E A</creatorcontrib><creatorcontrib>Ben-Hur, H</creatorcontrib><creatorcontrib>Hiller, Y</creatorcontrib><creatorcontrib>Wilchek, M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bayer, E A</au><au>Ben-Hur, H</au><au>Hiller, Y</au><au>Wilchek, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Postsecretory modifications of streptavidin</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1989-04-15</date><risdate>1989</risdate><volume>259</volume><issue>2</issue><spage>369</spage><epage>376</epage><pages>369-376</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>Streptavidin, an extracellular biotin-binding protein from Streptomyces avidinii, exhibits a multiplicity in its electrophoretic mobility pattern which depends both upon the conditions for growth of the bacterium and upon the protocol used in the purification of the protein. The observed structural heterogeneity appears to reflect the action of two types of postsecretory molecular events: proteolytic digestion of the intact Mr-18,000 subunit to a minimal molecular size (approx. Mr 14,000), and aggregation of the native tetramer into higher-order oligomeric forms. The extent of subunit degradation and/or tetrameric aggregation affects the capacity of a given streptavidin preparation to interact with biotin-conjugated proteins in different assay systems.</abstract><cop>England</cop><pmid>2719654</pmid><doi>10.1042/bj2590369</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0264-6021 |
| ispartof | Biochemical journal, 1989-04, Vol.259 (2), p.369-376 |
| issn | 0264-6021 1470-8728 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1138520 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Biotin - metabolism biotin-binding protein Electrophoresis, Polyacrylamide Gel Molecular Sequence Data Molecular Weight Protein Conformation Streptavidin |
| title | Postsecretory modifications of streptavidin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-11T00%3A03%3A34IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Postsecretory%20modifications%20of%20streptavidin&rft.jtitle=Biochemical%20journal&rft.au=Bayer,%20E%20A&rft.date=1989-04-15&rft.volume=259&rft.issue=2&rft.spage=369&rft.epage=376&rft.pages=369-376&rft.issn=0264-6021&rft.eissn=1470-8728&rft_id=info:doi/10.1042/bj2590369&rft_dat=%3Cproquest_pubme%3E78972855%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15323382&rft_id=info:pmid/2719654&rfr_iscdi=true |