Complete primary structure of the collagen-binding domain of bovine fibronectin
The complete amino acid sequence of the collagen‐binding domain of bovine plasma fibronectin has been determined. The fragment, generated by digestion of fibronectin with plasmin and chymotrypsin, contains 340 residues (260–599 of fibronectin) with threonine and tryptophan as the amino‐terminal and...
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| Veröffentlicht in: | European journal of biochemistry 1984-01, Vol.140 (2), p.235-243 |
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| creator | Skorstengaard, K Thogersen, H.C Petersen, T.E |
| description | The complete amino acid sequence of the collagen‐binding domain of bovine plasma fibronectin has been determined. The fragment, generated by digestion of fibronectin with plasmin and chymotrypsin, contains 340 residues (260–599 of fibronectin) with threonine and tryptophan as the amino‐terminal and carboxyl‐terminal amino acids, respectively. 24 half‐cystines and no cysteines are present in the sequence. Three glucosamine‐based oligosaccharide groups are attached to Asn‐399, Asn‐497 and to Asn‐511, respectively. Two of the three types (I and II) [Petersen et al. (1983) Proc. Natl Acad. Sci. USA 80, 137–141] of internal homology occur in the fragment, namely four of the at least twelve stretches of type I sequence homology, ‘fingers’, and two stretches of type II homology. The type I homology is present in two other plasmic fragments from fibronectin, while the type II homology has been found in the collagen‐binding domain only. |
| doi_str_mv | 10.1111/j.1432-1033.1984.tb08092.x |
| format | Article |
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The fragment, generated by digestion of fibronectin with plasmin and chymotrypsin, contains 340 residues (260–599 of fibronectin) with threonine and tryptophan as the amino‐terminal and carboxyl‐terminal amino acids, respectively. 24 half‐cystines and no cysteines are present in the sequence. Three glucosamine‐based oligosaccharide groups are attached to Asn‐399, Asn‐497 and to Asn‐511, respectively. Two of the three types (I and II) [Petersen et al. (1983) Proc. Natl Acad. Sci. USA 80, 137–141] of internal homology occur in the fragment, namely four of the at least twelve stretches of type I sequence homology, ‘fingers’, and two stretches of type II homology. 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Psychology ; Holoproteins ; Humans ; Other proteins ; Peptide Fragments - isolation & purification ; plasma ; Protein Binding ; Proteins ; Species Specificity</subject><ispartof>European journal of biochemistry, 1984-01, Vol.140 (2), p.235-243</ispartof><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5725-62d12619ca00d63fea1ffbdfbcd7bd5b1ea85d0f35d9463cf6b2eff35829a6d53</citedby><cites>FETCH-LOGICAL-c5725-62d12619ca00d63fea1ffbdfbcd7bd5b1ea85d0f35d9463cf6b2eff35829a6d53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9693912$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6714232$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Skorstengaard, K</creatorcontrib><creatorcontrib>Thogersen, H.C</creatorcontrib><creatorcontrib>Petersen, T.E</creatorcontrib><title>Complete primary structure of the collagen-binding domain of bovine fibronectin</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The complete amino acid sequence of the collagen‐binding domain of bovine plasma fibronectin has been determined. The fragment, generated by digestion of fibronectin with plasmin and chymotrypsin, contains 340 residues (260–599 of fibronectin) with threonine and tryptophan as the amino‐terminal and carboxyl‐terminal amino acids, respectively. 24 half‐cystines and no cysteines are present in the sequence. Three glucosamine‐based oligosaccharide groups are attached to Asn‐399, Asn‐497 and to Asn‐511, respectively. Two of the three types (I and II) [Petersen et al. (1983) Proc. Natl Acad. Sci. USA 80, 137–141] of internal homology occur in the fragment, namely four of the at least twelve stretches of type I sequence homology, ‘fingers’, and two stretches of type II homology. The type I homology is present in two other plasmic fragments from fibronectin, while the type II homology has been found in the collagen‐binding domain only.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>animal physiology</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Bridged-Ring Compounds - isolation & purification</subject><subject>Cattle</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>collagen</subject><subject>Collagen - metabolism</subject><subject>Disulfides - isolation & purification</subject><subject>fibronectin</subject><subject>Fibronectins - blood</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Holoproteins</subject><subject>Humans</subject><subject>Other proteins</subject><subject>Peptide Fragments - isolation & purification</subject><subject>plasma</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Species Specificity</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkEtv1DAURq2KqgyFn1ARIcQu4dqOnZgNglELlSp1Ubq2_Bw8SuLBTqD99ySaaLYIb66s79yHDkLvMFR4fh_3Fa4pKTFQWmHR1tWooQVBqqcztDlFL9AGANclEYy_RK9y3gMAF7y5QBe8wTWhZIPut7E_dG50xSGFXqXnIo9pMuOUXBF9Mf50hYldp3ZuKHUYbBh2hY29CsMS6_g7DK7wQac4ODOG4TU696rL7s1aL9HjzfWP7ffy7v7b7fbLXWlYQ1jJicWEY2EUgOXUO4W919ZrYxttmcZOtcyCp8yKmlPjuSbOz9-WCMUto5fow3HuIcVfk8uj7EM2br50cHHKssWARSPEP0FMWwENNDP46QiaFHNOzsvViMQgF-1yLxe3cnErF-1y1S6f5uardcuke2dPravnOX-_5iob1fmkBhPyCRNcUIEX7PMR-xM69_wfB8ib668PhC5e3h4neBWl2qV5yeMDAUyBMFY3dUv_ArAjqa8</recordid><startdate>19840101</startdate><enddate>19840101</enddate><creator>Skorstengaard, K</creator><creator>Thogersen, H.C</creator><creator>Petersen, T.E</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19840101</creationdate><title>Complete primary structure of the collagen-binding domain of bovine fibronectin</title><author>Skorstengaard, K ; Thogersen, H.C ; Petersen, T.E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5725-62d12619ca00d63fea1ffbdfbcd7bd5b1ea85d0f35d9463cf6b2eff35829a6d53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>animal physiology</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Bridged-Ring Compounds - isolation & purification</topic><topic>Cattle</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>collagen</topic><topic>Collagen - metabolism</topic><topic>Disulfides - isolation & purification</topic><topic>fibronectin</topic><topic>Fibronectins - blood</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Holoproteins</topic><topic>Humans</topic><topic>Other proteins</topic><topic>Peptide Fragments - isolation & purification</topic><topic>plasma</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Species Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Skorstengaard, K</creatorcontrib><creatorcontrib>Thogersen, H.C</creatorcontrib><creatorcontrib>Petersen, T.E</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Skorstengaard, K</au><au>Thogersen, H.C</au><au>Petersen, T.E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Complete primary structure of the collagen-binding domain of bovine fibronectin</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1984-01-01</date><risdate>1984</risdate><volume>140</volume><issue>2</issue><spage>235</spage><epage>243</epage><pages>235-243</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>The complete amino acid sequence of the collagen‐binding domain of bovine plasma fibronectin has been determined. The fragment, generated by digestion of fibronectin with plasmin and chymotrypsin, contains 340 residues (260–599 of fibronectin) with threonine and tryptophan as the amino‐terminal and carboxyl‐terminal amino acids, respectively. 24 half‐cystines and no cysteines are present in the sequence. Three glucosamine‐based oligosaccharide groups are attached to Asn‐399, Asn‐497 and to Asn‐511, respectively. Two of the three types (I and II) [Petersen et al. (1983) Proc. Natl Acad. Sci. USA 80, 137–141] of internal homology occur in the fragment, namely four of the at least twelve stretches of type I sequence homology, ‘fingers’, and two stretches of type II homology. The type I homology is present in two other plasmic fragments from fibronectin, while the type II homology has been found in the collagen‐binding domain only.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>6714232</pmid><doi>10.1111/j.1432-1033.1984.tb08092.x</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | European journal of biochemistry, 1984-01, Vol.140 (2), p.235-243 |
| issn | 0014-2956 1432-1033 |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry animal physiology Animals Binding Sites Biological and medical sciences Bridged-Ring Compounds - isolation & purification Cattle Chemical Phenomena Chemistry collagen Collagen - metabolism Disulfides - isolation & purification fibronectin Fibronectins - blood Fundamental and applied biological sciences. Psychology Holoproteins Humans Other proteins Peptide Fragments - isolation & purification plasma Protein Binding Proteins Species Specificity |
| title | Complete primary structure of the collagen-binding domain of bovine fibronectin |
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