Identification of feline herpesvirus type 1-hemagglutinin
The crude hemagglutinin of feline herpesvirus type 1 (FHV-1), solubilized from infected fcwf-4 cells by detergents, was partially purified by three kinds of chromatographic methods. Lectin-affinity chromatography showed the hemagglutination (HA) activity in fractions, which was bound to Concanavalin...
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| Veröffentlicht in: | Japanese journal of veterinary science 1989/06/15, Vol.51(3), pp.607-612 |
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| creator | Horimoto, T. (Tokyo Univ. (Japan). Faculty of Agriculture) Kasaoka, T Tuchiya, K Takahashi, E |
| description | The crude hemagglutinin of feline herpesvirus type 1 (FHV-1), solubilized from infected fcwf-4 cells by detergents, was partially purified by three kinds of chromatographic methods. Lectin-affinity chromatography showed the hemagglutination (HA) activity in fractions, which was bound to Concanavalin A-sepharose and then eluted by α-methyl D-mannoside, suggesting that the hemagglutinin might include a glycoprotein. Ion-exchange and gel-exclusion chromatographies were also capable of purifying the detergent-soluble crude hemagglutinin. When peak HA fractions, which were obtained from each of the three procedures, were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the gel-exclusion chromatography was the most effective method. Electrophoreic analysis also showed only one band of 59, 000 (59K) molecular weight protein, which was commonly observed in the three partially purified hemagglutinins with silver staining. In addition, the 59K protein band was clearly recognized in immunoblot analysis of the infected cell lysates using infected cat serum. These observations suggest that the FHV-1 detergent-soluble hemagglutinin from infected fcwf-4 cells may be closely related to a 59K immunogenic glycoprotein. |
| doi_str_mv | 10.1292/jvms1939.51.607 |
| format | Article |
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(Tokyo Univ. (Japan). Faculty of Agriculture) ; Kasaoka, T ; Tuchiya, K ; Takahashi, E</creator><creatorcontrib>Horimoto, T. (Tokyo Univ. (Japan). Faculty of Agriculture) ; Kasaoka, T ; Tuchiya, K ; Takahashi, E</creatorcontrib><description>The crude hemagglutinin of feline herpesvirus type 1 (FHV-1), solubilized from infected fcwf-4 cells by detergents, was partially purified by three kinds of chromatographic methods. Lectin-affinity chromatography showed the hemagglutination (HA) activity in fractions, which was bound to Concanavalin A-sepharose and then eluted by α-methyl D-mannoside, suggesting that the hemagglutinin might include a glycoprotein. Ion-exchange and gel-exclusion chromatographies were also capable of purifying the detergent-soluble crude hemagglutinin. When peak HA fractions, which were obtained from each of the three procedures, were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the gel-exclusion chromatography was the most effective method. Electrophoreic analysis also showed only one band of 59, 000 (59K) molecular weight protein, which was commonly observed in the three partially purified hemagglutinins with silver staining. In addition, the 59K protein band was clearly recognized in immunoblot analysis of the infected cell lysates using infected cat serum. 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(Tokyo Univ. (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Kasaoka, T</creatorcontrib><creatorcontrib>Tuchiya, K</creatorcontrib><creatorcontrib>Takahashi, E</creatorcontrib><title>Identification of feline herpesvirus type 1-hemagglutinin</title><title>Japanese journal of veterinary science</title><addtitle>The Japanese Journal of Veterinary Science</addtitle><description>The crude hemagglutinin of feline herpesvirus type 1 (FHV-1), solubilized from infected fcwf-4 cells by detergents, was partially purified by three kinds of chromatographic methods. Lectin-affinity chromatography showed the hemagglutination (HA) activity in fractions, which was bound to Concanavalin A-sepharose and then eluted by α-methyl D-mannoside, suggesting that the hemagglutinin might include a glycoprotein. Ion-exchange and gel-exclusion chromatographies were also capable of purifying the detergent-soluble crude hemagglutinin. When peak HA fractions, which were obtained from each of the three procedures, were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the gel-exclusion chromatography was the most effective method. Electrophoreic analysis also showed only one band of 59, 000 (59K) molecular weight protein, which was commonly observed in the three partially purified hemagglutinins with silver staining. In addition, the 59K protein band was clearly recognized in immunoblot analysis of the infected cell lysates using infected cat serum. These observations suggest that the FHV-1 detergent-soluble hemagglutinin from infected fcwf-4 cells may be closely related to a 59K immunogenic glycoprotein.</description><subject>AGGLUTININE</subject><subject>AGGLUTININS</subject><subject>AGLUTININAS</subject><subject>ANIMAL VIRUSES</subject><subject>Animals</subject><subject>CATS</subject><subject>Cells, Cultured</subject><subject>CHAT</subject><subject>CHROMATOGRAPHIE</subject><subject>CHROMATOGRAPHY</subject><subject>Chromatography, Gel</subject><subject>CROMATOGRAFIA</subject><subject>Detergents</subject><subject>ELECTROFORESIS</subject><subject>ELECTROPHORESE</subject><subject>ELECTROPHORESIS</subject><subject>feline herpesvirus type 1</subject><subject>GATO</subject><subject>GLICOPROTEINAS</subject><subject>glycoprotein</subject><subject>GLYCOPROTEINE</subject><subject>GLYCOPROTEINS</subject><subject>hemagglutinin</subject><subject>Hemagglutinins, Viral - isolation & purification</subject><subject>Herpesviridae - immunology</subject><subject>HERPETOVIRIDAE</subject><subject>Membrane Glycoproteins - isolation & purification</subject><subject>Molecular Weight</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>Solubility</subject><subject>VIRUS DE LOS ANIMALES</subject><subject>VIRUS DES ANIMAUX</subject><issn>0021-5295</issn><issn>1881-1442</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkEtLxDAURoMoOj7WgiB05a5jbto0yVJ8jgi60HVI25tOhj7GpB2Yf2-l44CbZHG-exaHkEugc2CK3a42TQCVqDmHeUbFAZmBlBBDmrJDMqOUQcyZ4ifkNIQVpamSVByTYyYyAJ7MiFqU2PbOusL0rmujzkYWa9ditES_xrBxfghRv11jBPESG1NV9dC71rXn5MiaOuDF7j8jX0-Pn_cv8dv78-L-7i0uUkj6OOM2k4ksjJR5icJQapBlOROmVJSWGeVGIAKTFlRKFRdpXliUqckVcIsiOSM3k3ftu-8BQ68bFwqsa9NiNwQtFCSMpnIc3k7DwncheLR67V1j_FYD1b-x9F8szUGPscaL6516yBss9_tdnZE_THwVelPhnhvfu6LGf75kekbtHhdL4zW2o-Zq0ljTaVN5F_Trh2IU-FjoByQHhjE</recordid><startdate>19890601</startdate><enddate>19890601</enddate><creator>Horimoto, T. (Tokyo Univ. (Japan). Faculty of Agriculture)</creator><creator>Kasaoka, T</creator><creator>Tuchiya, K</creator><creator>Takahashi, E</creator><general>JAPANESE SOCIETY OF VETERINARY SCIENCE</general><scope>FBQ</scope><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>19890601</creationdate><title>Identification of feline herpesvirus type 1-hemagglutinin</title><author>Horimoto, T. (Tokyo Univ. (Japan). Faculty of Agriculture) ; Kasaoka, T ; Tuchiya, K ; Takahashi, E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c413t-65f6838ca88bde7a00ae26b27ad900d605a7ee128f19409574bcfe84ab915fe73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>AGGLUTININE</topic><topic>AGGLUTININS</topic><topic>AGLUTININAS</topic><topic>ANIMAL VIRUSES</topic><topic>Animals</topic><topic>CATS</topic><topic>Cells, Cultured</topic><topic>CHAT</topic><topic>CHROMATOGRAPHIE</topic><topic>CHROMATOGRAPHY</topic><topic>Chromatography, Gel</topic><topic>CROMATOGRAFIA</topic><topic>Detergents</topic><topic>ELECTROFORESIS</topic><topic>ELECTROPHORESE</topic><topic>ELECTROPHORESIS</topic><topic>feline herpesvirus type 1</topic><topic>GATO</topic><topic>GLICOPROTEINAS</topic><topic>glycoprotein</topic><topic>GLYCOPROTEINE</topic><topic>GLYCOPROTEINS</topic><topic>hemagglutinin</topic><topic>Hemagglutinins, Viral - isolation & purification</topic><topic>Herpesviridae - immunology</topic><topic>HERPETOVIRIDAE</topic><topic>Membrane Glycoproteins - isolation & purification</topic><topic>Molecular Weight</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>Solubility</topic><topic>VIRUS DE LOS ANIMALES</topic><topic>VIRUS DES ANIMAUX</topic><toplevel>online_resources</toplevel><creatorcontrib>Horimoto, T. (Tokyo Univ. (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Kasaoka, T</creatorcontrib><creatorcontrib>Tuchiya, K</creatorcontrib><creatorcontrib>Takahashi, E</creatorcontrib><collection>AGRIS</collection><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>Japanese journal of veterinary science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Horimoto, T. (Tokyo Univ. (Japan). Faculty of Agriculture)</au><au>Kasaoka, T</au><au>Tuchiya, K</au><au>Takahashi, E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of feline herpesvirus type 1-hemagglutinin</atitle><jtitle>Japanese journal of veterinary science</jtitle><addtitle>The Japanese Journal of Veterinary Science</addtitle><date>1989-06-01</date><risdate>1989</risdate><volume>51</volume><issue>3</issue><spage>607</spage><epage>612</epage><pages>607-612</pages><issn>0021-5295</issn><eissn>1881-1442</eissn><abstract>The crude hemagglutinin of feline herpesvirus type 1 (FHV-1), solubilized from infected fcwf-4 cells by detergents, was partially purified by three kinds of chromatographic methods. Lectin-affinity chromatography showed the hemagglutination (HA) activity in fractions, which was bound to Concanavalin A-sepharose and then eluted by α-methyl D-mannoside, suggesting that the hemagglutinin might include a glycoprotein. Ion-exchange and gel-exclusion chromatographies were also capable of purifying the detergent-soluble crude hemagglutinin. When peak HA fractions, which were obtained from each of the three procedures, were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the gel-exclusion chromatography was the most effective method. Electrophoreic analysis also showed only one band of 59, 000 (59K) molecular weight protein, which was commonly observed in the three partially purified hemagglutinins with silver staining. In addition, the 59K protein band was clearly recognized in immunoblot analysis of the infected cell lysates using infected cat serum. These observations suggest that the FHV-1 detergent-soluble hemagglutinin from infected fcwf-4 cells may be closely related to a 59K immunogenic glycoprotein.</abstract><cop>Japan</cop><pub>JAPANESE SOCIETY OF VETERINARY SCIENCE</pub><pmid>2761153</pmid><doi>10.1292/jvms1939.51.607</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Japanese Journal of Veterinary Science, 1989/06/15, Vol.51(3), pp.607-612 |
| issn | 0021-5295 1881-1442 |
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| source | MEDLINE; J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; AgriKnowledge（アグリナレッジ）AGROLib |
| subjects | AGGLUTININE AGGLUTININS AGLUTININAS ANIMAL VIRUSES Animals CATS Cells, Cultured CHAT CHROMATOGRAPHIE CHROMATOGRAPHY Chromatography, Gel CROMATOGRAFIA Detergents ELECTROFORESIS ELECTROPHORESE ELECTROPHORESIS feline herpesvirus type 1 GATO GLICOPROTEINAS glycoprotein GLYCOPROTEINE GLYCOPROTEINS hemagglutinin Hemagglutinins, Viral - isolation & purification Herpesviridae - immunology HERPETOVIRIDAE Membrane Glycoproteins - isolation & purification Molecular Weight PURIFICACION PURIFICATION Solubility VIRUS DE LOS ANIMALES VIRUS DES ANIMAUX |
| title | Identification of feline herpesvirus type 1-hemagglutinin |
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