Yolk vitronectin. Purification and differences from its blood homologue in molecular size, heparin binding, collagen binding, and bound carbohydrate
This is the first report on a unique vitronectin molecule, yolk vitronectin, which is similar to its blood homologue in cell spreading activity but different in molecular size, bound carbohydrate, and heparin and collagen binding activity. Yolk vitronectin was purified 2,500-fold from chick egg yolk...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-12, Vol.267 (34), p.24863-24870 |
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| container_title | The Journal of biological chemistry |
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| creator | Nagano, Y. (Ochanomizu University, Bunkyo-ku, Tokyo, Japan) Hamano, T Nakashima, N Ishikawa, M Miyazaki, K Hayashi, M |
| description | This is the first report on a unique vitronectin molecule, yolk vitronectin, which is similar to its blood homologue in cell spreading activity but different in molecular size, bound carbohydrate, and heparin and collagen binding activity. Yolk vitronectin was purified 2,500-fold from chick egg yolk by a combination of hydroxylapatite, DEAE-cellulose, and anti-vitronectin-Sepharose column chromatographies. In SDS-polyacrylamide gel electrophoresis under reducing conditions, yolk vitronectin was separated into 54- and 45-kDa bands, which are 16 and 25 kDa smaller, respectively, than the 70-kDa major band of chick blood vitronectin. The 54-kDa band shares the same NH2-terminal sequence as chick blood vitronectin. In contrast, the NH2-terminal sequence of the 45-kDa band is somewhat homologous with the internal sequences of mammalian vitronectins beginning at the 50th amino acid from the NH2 terminus. The bound carbohydrate of the 54- and 45-kDa species of yolk vitronectin is similar to, but distinct from, that of blood vitronectin. Unlike blood vitronectin, yolk vitronectin cannot bind to either heparin or collagen |
| doi_str_mv | 10.1016/s0021-9258(18)35843-5 |
| format | Article |
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Purification and differences from its blood homologue in molecular size, heparin binding, collagen binding, and bound carbohydrate</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Nagano, Y. (Ochanomizu University, Bunkyo-ku, Tokyo, Japan) ; Hamano, T ; Nakashima, N ; Ishikawa, M ; Miyazaki, K ; Hayashi, M</creator><creatorcontrib>Nagano, Y. (Ochanomizu University, Bunkyo-ku, Tokyo, Japan) ; Hamano, T ; Nakashima, N ; Ishikawa, M ; Miyazaki, K ; Hayashi, M</creatorcontrib><description>This is the first report on a unique vitronectin molecule, yolk vitronectin, which is similar to its blood homologue in cell spreading activity but different in molecular size, bound carbohydrate, and heparin and collagen binding activity. Yolk vitronectin was purified 2,500-fold from chick egg yolk by a combination of hydroxylapatite, DEAE-cellulose, and anti-vitronectin-Sepharose column chromatographies. In SDS-polyacrylamide gel electrophoresis under reducing conditions, yolk vitronectin was separated into 54- and 45-kDa bands, which are 16 and 25 kDa smaller, respectively, than the 70-kDa major band of chick blood vitronectin. The 54-kDa band shares the same NH2-terminal sequence as chick blood vitronectin. In contrast, the NH2-terminal sequence of the 45-kDa band is somewhat homologous with the internal sequences of mammalian vitronectins beginning at the 50th amino acid from the NH2 terminus. The bound carbohydrate of the 54- and 45-kDa species of yolk vitronectin is similar to, but distinct from, that of blood vitronectin. Unlike blood vitronectin, yolk vitronectin cannot bind to either heparin or collagen</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(18)35843-5</identifier><identifier>PMID: 1280270</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Binding Sites ; Biological and medical sciences ; Blood Proteins - isolation & purification ; Blotting, Western ; Carbohydrates - analysis ; Chickens ; Chromatography ; Chromatography, Affinity ; Chromatography, DEAE-Cellulose ; Collagen - metabolism ; Durapatite ; Egg White ; Egg Yolk ; Electrophoresis, Polyacrylamide Gel ; EMBRIONES ANIMALES ; EMBRYON ANIMAL ; Female ; Fibronectins - isolation & purification ; Fibronectins - metabolism ; Fundamental and applied biological sciences. Psychology ; GLICOPROTEINAS ; GLYCOPROTEINE ; Glycoproteins ; Glycoproteins - blood ; Glycoproteins - isolation & purification ; Glycoproteins - metabolism ; Heparin - metabolism ; Humans ; Hydroxyapatites ; Mice ; Molecular Sequence Data ; Molecular Weight ; POLLITO ; POUSSIN ; Proteins ; PURIFICACION ; PURIFICATION ; Rabbits ; Sequence Homology, Amino Acid ; VITELLUS ; Vitronectin ; YEMA DE HUEVO</subject><ispartof>The Journal of biological chemistry, 1992-12, Vol.267 (34), p.24863-24870</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4095-27fdb48235b16c541320b593ce6b99bd4f2d4ae9ba7a88ebad6e6acdd2a08413</citedby><cites>FETCH-LOGICAL-c4095-27fdb48235b16c541320b593ce6b99bd4f2d4ae9ba7a88ebad6e6acdd2a08413</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4480985$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1280270$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nagano, Y. (Ochanomizu University, Bunkyo-ku, Tokyo, Japan)</creatorcontrib><creatorcontrib>Hamano, T</creatorcontrib><creatorcontrib>Nakashima, N</creatorcontrib><creatorcontrib>Ishikawa, M</creatorcontrib><creatorcontrib>Miyazaki, K</creatorcontrib><creatorcontrib>Hayashi, M</creatorcontrib><title>Yolk vitronectin. Purification and differences from its blood homologue in molecular size, heparin binding, collagen binding, and bound carbohydrate</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>This is the first report on a unique vitronectin molecule, yolk vitronectin, which is similar to its blood homologue in cell spreading activity but different in molecular size, bound carbohydrate, and heparin and collagen binding activity. Yolk vitronectin was purified 2,500-fold from chick egg yolk by a combination of hydroxylapatite, DEAE-cellulose, and anti-vitronectin-Sepharose column chromatographies. In SDS-polyacrylamide gel electrophoresis under reducing conditions, yolk vitronectin was separated into 54- and 45-kDa bands, which are 16 and 25 kDa smaller, respectively, than the 70-kDa major band of chick blood vitronectin. The 54-kDa band shares the same NH2-terminal sequence as chick blood vitronectin. In contrast, the NH2-terminal sequence of the 45-kDa band is somewhat homologous with the internal sequences of mammalian vitronectins beginning at the 50th amino acid from the NH2 terminus. The bound carbohydrate of the 54- and 45-kDa species of yolk vitronectin is similar to, but distinct from, that of blood vitronectin. Unlike blood vitronectin, yolk vitronectin cannot bind to either heparin or collagen</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Blood Proteins - isolation & purification</subject><subject>Blotting, Western</subject><subject>Carbohydrates - analysis</subject><subject>Chickens</subject><subject>Chromatography</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, DEAE-Cellulose</subject><subject>Collagen - metabolism</subject><subject>Durapatite</subject><subject>Egg White</subject><subject>Egg Yolk</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>EMBRIONES ANIMALES</subject><subject>EMBRYON ANIMAL</subject><subject>Female</subject><subject>Fibronectins - isolation & purification</subject><subject>Fibronectins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GLICOPROTEINAS</subject><subject>GLYCOPROTEINE</subject><subject>Glycoproteins</subject><subject>Glycoproteins - blood</subject><subject>Glycoproteins - isolation & purification</subject><subject>Glycoproteins - metabolism</subject><subject>Heparin - metabolism</subject><subject>Humans</subject><subject>Hydroxyapatites</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>POLLITO</subject><subject>POUSSIN</subject><subject>Proteins</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>Rabbits</subject><subject>Sequence Homology, Amino Acid</subject><subject>VITELLUS</subject><subject>Vitronectin</subject><subject>YEMA DE HUEVO</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkV1rFTEQhhdR6mn1DwiFXIhU6NZ87iaXUvyCgkIr6FXIx-xudHdzTHaV-jv8weZ4Dq25mISZZ94M71TVKcEXBJPmVcaYklpRIc-IfMmE5KwWD6oNwZLVTJAvD6vNHfK4Os75Gy6HK3JUHREqMW3xpvrzNY7f0c-wpDiDW8J8gT6tKXTBmSXEGZnZIx-6DhLMDjLqUpxQWDKyY4weDXGKY-xXQGFG5QluHU1COfyGczTA1qSSt2H2Ye7PkYvjaHr4L7OTt3Et0Zlk43Drk1ngSfWoM2OGp4f7pLp5--bm8n199fHdh8vXV7XjWImatp23XFImLGmc4IRRbIViDhqrlPW8o54bUNa0RkqwxjfQGOc9NVgW-qR6sZfdpvhjhbzoKWQHZcYZ4pp1y5hgDNMCij3oUsw5Qae3KUwm3WqC9W4Z-nrntN45rYnU_5ahRek7PXyw2gn8fdfe_VJ_fqib7MzYJTO7kO8wziVWUtxjQ-iHXyGBtiG6ASZNm1YzrimXDSvYsz3WmahNn4rS52vFcdMSxf4CKjqpKQ</recordid><startdate>19921205</startdate><enddate>19921205</enddate><creator>Nagano, Y. (Ochanomizu University, Bunkyo-ku, Tokyo, Japan)</creator><creator>Hamano, T</creator><creator>Nakashima, N</creator><creator>Ishikawa, M</creator><creator>Miyazaki, K</creator><creator>Hayashi, M</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>FBQ</scope><scope>IQODW</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>19921205</creationdate><title>Yolk vitronectin. Purification and differences from its blood homologue in molecular size, heparin binding, collagen binding, and bound carbohydrate</title><author>Nagano, Y. (Ochanomizu University, Bunkyo-ku, Tokyo, Japan) ; Hamano, T ; Nakashima, N ; Ishikawa, M ; Miyazaki, K ; Hayashi, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4095-27fdb48235b16c541320b593ce6b99bd4f2d4ae9ba7a88ebad6e6acdd2a08413</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Blood Proteins - isolation & purification</topic><topic>Blotting, Western</topic><topic>Carbohydrates - analysis</topic><topic>Chickens</topic><topic>Chromatography</topic><topic>Chromatography, Affinity</topic><topic>Chromatography, DEAE-Cellulose</topic><topic>Collagen - metabolism</topic><topic>Durapatite</topic><topic>Egg White</topic><topic>Egg Yolk</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>EMBRIONES ANIMALES</topic><topic>EMBRYON ANIMAL</topic><topic>Female</topic><topic>Fibronectins - isolation & purification</topic><topic>Fibronectins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GLICOPROTEINAS</topic><topic>GLYCOPROTEINE</topic><topic>Glycoproteins</topic><topic>Glycoproteins - blood</topic><topic>Glycoproteins - isolation & purification</topic><topic>Glycoproteins - metabolism</topic><topic>Heparin - metabolism</topic><topic>Humans</topic><topic>Hydroxyapatites</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>POLLITO</topic><topic>POUSSIN</topic><topic>Proteins</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>Rabbits</topic><topic>Sequence Homology, Amino Acid</topic><topic>VITELLUS</topic><topic>Vitronectin</topic><topic>YEMA DE HUEVO</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nagano, Y. (Ochanomizu University, Bunkyo-ku, Tokyo, Japan)</creatorcontrib><creatorcontrib>Hamano, T</creatorcontrib><creatorcontrib>Nakashima, N</creatorcontrib><creatorcontrib>Ishikawa, M</creatorcontrib><creatorcontrib>Miyazaki, K</creatorcontrib><creatorcontrib>Hayashi, M</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nagano, Y. (Ochanomizu University, Bunkyo-ku, Tokyo, Japan)</au><au>Hamano, T</au><au>Nakashima, N</au><au>Ishikawa, M</au><au>Miyazaki, K</au><au>Hayashi, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Yolk vitronectin. Purification and differences from its blood homologue in molecular size, heparin binding, collagen binding, and bound carbohydrate</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-12-05</date><risdate>1992</risdate><volume>267</volume><issue>34</issue><spage>24863</spage><epage>24870</epage><pages>24863-24870</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>This is the first report on a unique vitronectin molecule, yolk vitronectin, which is similar to its blood homologue in cell spreading activity but different in molecular size, bound carbohydrate, and heparin and collagen binding activity. Yolk vitronectin was purified 2,500-fold from chick egg yolk by a combination of hydroxylapatite, DEAE-cellulose, and anti-vitronectin-Sepharose column chromatographies. In SDS-polyacrylamide gel electrophoresis under reducing conditions, yolk vitronectin was separated into 54- and 45-kDa bands, which are 16 and 25 kDa smaller, respectively, than the 70-kDa major band of chick blood vitronectin. The 54-kDa band shares the same NH2-terminal sequence as chick blood vitronectin. In contrast, the NH2-terminal sequence of the 45-kDa band is somewhat homologous with the internal sequences of mammalian vitronectins beginning at the 50th amino acid from the NH2 terminus. The bound carbohydrate of the 54- and 45-kDa species of yolk vitronectin is similar to, but distinct from, that of blood vitronectin. Unlike blood vitronectin, yolk vitronectin cannot bind to either heparin or collagen</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1280270</pmid><doi>10.1016/s0021-9258(18)35843-5</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1992-12, Vol.267 (34), p.24863-24870 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73353302 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Binding Sites Biological and medical sciences Blood Proteins - isolation & purification Blotting, Western Carbohydrates - analysis Chickens Chromatography Chromatography, Affinity Chromatography, DEAE-Cellulose Collagen - metabolism Durapatite Egg White Egg Yolk Electrophoresis, Polyacrylamide Gel EMBRIONES ANIMALES EMBRYON ANIMAL Female Fibronectins - isolation & purification Fibronectins - metabolism Fundamental and applied biological sciences. Psychology GLICOPROTEINAS GLYCOPROTEINE Glycoproteins Glycoproteins - blood Glycoproteins - isolation & purification Glycoproteins - metabolism Heparin - metabolism Humans Hydroxyapatites Mice Molecular Sequence Data Molecular Weight POLLITO POUSSIN Proteins PURIFICACION PURIFICATION Rabbits Sequence Homology, Amino Acid VITELLUS Vitronectin YEMA DE HUEVO |
| title | Yolk vitronectin. Purification and differences from its blood homologue in molecular size, heparin binding, collagen binding, and bound carbohydrate |
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