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Rapid purification of pertussis toxin (PT) and filamentous hemagglutinin (FHA) by cation-exchange chromatography
Pertussis toxin (PT) and filamentous hemagglutinin (FHA) were purified from culture supernatant of Bordetella pertussis Saadet and Tohama strains, using CM-Sepharose CL-6B cation-exchange chromatography. By the rapid purification method described here, both proteins were separately eluted from the s...
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| Published in: | Vaccine 2004-03, Vol.22 (11), p.1570-1575 |
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| container_end_page | 1575 |
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| creator | Ozcengiz, Erkan Kilinç, Kamer Büyüktanir, Ozlem Günalp, Ayfer |
| description | Pertussis toxin (PT) and filamentous hemagglutinin (FHA) were purified from culture supernatant of
Bordetella pertussis Saadet and Tohama strains, using CM-Sepharose CL-6B cation-exchange chromatography. By the rapid purification method described here, both proteins were separately eluted from the same column in pure forms. The PT and FHA in the extract of culture supernatant were bounded to CM-Sepharose CL-6B cation-exchange column in 50
mM phosphate buffer containing 2
M urea (Buffer A), pH 6.0. Then the PT was eluted from the column with Buffer A (pH 7.4) and after elution of the PT, the FHA was eluted with 0.5
M NaCl in 50
mM phosphate buffer. Pertussis toxin and filamentous haemagglutinin purified by this procedure were electrophoretically and immunologically identical to the reference preparations. |
| doi_str_mv | 10.1016/j.vaccine.2003.09.040 |
| format | article |
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Bordetella pertussis Saadet and Tohama strains, using CM-Sepharose CL-6B cation-exchange chromatography. By the rapid purification method described here, both proteins were separately eluted from the same column in pure forms. The PT and FHA in the extract of culture supernatant were bounded to CM-Sepharose CL-6B cation-exchange column in 50
mM phosphate buffer containing 2
M urea (Buffer A), pH 6.0. Then the PT was eluted from the column with Buffer A (pH 7.4) and after elution of the PT, the FHA was eluted with 0.5
M NaCl in 50
mM phosphate buffer. Pertussis toxin and filamentous haemagglutinin purified by this procedure were electrophoretically and immunologically identical to the reference preparations.</description><identifier>ISSN: 0264-410X</identifier><identifier>EISSN: 1873-2518</identifier><identifier>DOI: 10.1016/j.vaccine.2003.09.040</identifier><identifier>PMID: 15063583</identifier><identifier>CODEN: VACCDE</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Animals ; Applied microbiology ; Biological and medical sciences ; Bordetella pertussis ; Bordetella pertussis - growth & development ; Bordetella pertussis - metabolism ; Chickens ; Chromatography ; Chromatography, Ion Exchange ; Electrophoresis, Polyacrylamide Gel ; Enzyme-Linked Immunosorbent Assay ; Enzymes ; Erythrocytes - immunology ; Filamentous hemagglutinin ; Fundamental and applied biological sciences. Psychology ; Hemagglutination Inhibition Tests ; Hemagglutinins - isolation & purification ; Histamine - pharmacology ; In Vitro Techniques ; Leukocytosis ; Methods ; Mice ; Microbiology ; Molecular weight ; Pertussis toxin ; Pertussis Toxin - isolation & purification ; Proteins ; Purification ; Sepharose - analogs & derivatives ; Sodium chloride ; Studies ; Toxins ; Urea ; Vaccine ; Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies (general aspects) ; Whooping cough</subject><ispartof>Vaccine, 2004-03, Vol.22 (11), p.1570-1575</ispartof><rights>2003 Elsevier Ltd</rights><rights>2004 INIST-CNRS</rights><rights>Copyright Elsevier Limited Mar 29, 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c450t-de3d0253d331f84f6223a96b3618af05b2af8e5409a2c185d22d620b85d32d2f3</citedby><cites>FETCH-LOGICAL-c450t-de3d0253d331f84f6223a96b3618af05b2af8e5409a2c185d22d620b85d32d2f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15601562$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15063583$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ozcengiz, Erkan</creatorcontrib><creatorcontrib>Kilinç, Kamer</creatorcontrib><creatorcontrib>Büyüktanir, Ozlem</creatorcontrib><creatorcontrib>Günalp, Ayfer</creatorcontrib><title>Rapid purification of pertussis toxin (PT) and filamentous hemagglutinin (FHA) by cation-exchange chromatography</title><title>Vaccine</title><addtitle>Vaccine</addtitle><description>Pertussis toxin (PT) and filamentous hemagglutinin (FHA) were purified from culture supernatant of
Bordetella pertussis Saadet and Tohama strains, using CM-Sepharose CL-6B cation-exchange chromatography. By the rapid purification method described here, both proteins were separately eluted from the same column in pure forms. The PT and FHA in the extract of culture supernatant were bounded to CM-Sepharose CL-6B cation-exchange column in 50
mM phosphate buffer containing 2
M urea (Buffer A), pH 6.0. Then the PT was eluted from the column with Buffer A (pH 7.4) and after elution of the PT, the FHA was eluted with 0.5
M NaCl in 50
mM phosphate buffer. Pertussis toxin and filamentous haemagglutinin purified by this procedure were electrophoretically and immunologically identical to the reference preparations.</description><subject>Animals</subject><subject>Applied microbiology</subject><subject>Biological and medical sciences</subject><subject>Bordetella pertussis</subject><subject>Bordetella pertussis - growth & development</subject><subject>Bordetella pertussis - metabolism</subject><subject>Chickens</subject><subject>Chromatography</subject><subject>Chromatography, Ion Exchange</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Enzymes</subject><subject>Erythrocytes - immunology</subject><subject>Filamentous hemagglutinin</subject><subject>Fundamental and applied biological sciences. 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Academic</collection><jtitle>Vaccine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ozcengiz, Erkan</au><au>Kilinç, Kamer</au><au>Büyüktanir, Ozlem</au><au>Günalp, Ayfer</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rapid purification of pertussis toxin (PT) and filamentous hemagglutinin (FHA) by cation-exchange chromatography</atitle><jtitle>Vaccine</jtitle><addtitle>Vaccine</addtitle><date>2004-03-29</date><risdate>2004</risdate><volume>22</volume><issue>11</issue><spage>1570</spage><epage>1575</epage><pages>1570-1575</pages><issn>0264-410X</issn><eissn>1873-2518</eissn><coden>VACCDE</coden><abstract>Pertussis toxin (PT) and filamentous hemagglutinin (FHA) were purified from culture supernatant of
Bordetella pertussis Saadet and Tohama strains, using CM-Sepharose CL-6B cation-exchange chromatography. By the rapid purification method described here, both proteins were separately eluted from the same column in pure forms. The PT and FHA in the extract of culture supernatant were bounded to CM-Sepharose CL-6B cation-exchange column in 50
mM phosphate buffer containing 2
M urea (Buffer A), pH 6.0. Then the PT was eluted from the column with Buffer A (pH 7.4) and after elution of the PT, the FHA was eluted with 0.5
M NaCl in 50
mM phosphate buffer. Pertussis toxin and filamentous haemagglutinin purified by this procedure were electrophoretically and immunologically identical to the reference preparations.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>15063583</pmid><doi>10.1016/j.vaccine.2003.09.040</doi><tpages>6</tpages></addata></record> |
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| ispartof | Vaccine, 2004-03, Vol.22 (11), p.1570-1575 |
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| source | ScienceDirect Journals |
| subjects | Animals Applied microbiology Biological and medical sciences Bordetella pertussis Bordetella pertussis - growth & development Bordetella pertussis - metabolism Chickens Chromatography Chromatography, Ion Exchange Electrophoresis, Polyacrylamide Gel Enzyme-Linked Immunosorbent Assay Enzymes Erythrocytes - immunology Filamentous hemagglutinin Fundamental and applied biological sciences. Psychology Hemagglutination Inhibition Tests Hemagglutinins - isolation & purification Histamine - pharmacology In Vitro Techniques Leukocytosis Methods Mice Microbiology Molecular weight Pertussis toxin Pertussis Toxin - isolation & purification Proteins Purification Sepharose - analogs & derivatives Sodium chloride Studies Toxins Urea Vaccine Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies (general aspects) Whooping cough |
| title | Rapid purification of pertussis toxin (PT) and filamentous hemagglutinin (FHA) by cation-exchange chromatography |
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