Binding of Thyroxine to Pig Transthyretin, its cDNA Structure, and Other Properties
Thyroxine binding to proteins in pig plasma during electrophoresis was observed in the albumin, but not in the prealbumin and post‐albumin regions. Transthyretin could be identified in medium from in vitro pig choroid plexus incubations by size and number of subunits and a very high rate of synthesi...
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Veröffentlicht in: | European journal of biochemistry 1995-06, Vol.230 (3), p.977-986 |
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creator | Duan, Wei Richardson, Samantha J. Köhrle, Josef Chang, Linus Southwell, Bridget R. Harms, Paul J. Brack, Charlotte M. Pettersson, Tom M. Schreiber, Gerhard |
description | Thyroxine binding to proteins in pig plasma during electrophoresis was observed in the albumin, but not in the prealbumin and post‐albumin regions.
Transthyretin could be identified in medium from in vitro pig choroid plexus incubations by size and number of subunits and a very high rate of synthesis and secretion. Its electrophoretic mobility was intermediate between that of thyroxine‐binding globulin and albumin. It bound thyroxine, retinol‐binding protein, anti‐(rat transthyretin) antibodies and behaved similarly to transthyretins from other vertebrate species when plasma was extracted with phenol. Inhibition experiments with the synthetic flavonoid F 21388, analysing the binding of thyroxine, suggested that transthyretin is not a major thyroxine carrier in the bloodstream of pigs.
Cloning and sequencing of transthyretin cDNA from both choroid plexus and liver showed that the same transthyretin mRNA is expressed in pig choroid plexus and liver. The amino acid sequence derived from the nucleotide sequence revealed that pig transthyretin differs from the transthyretins of all other studied vertebrate species by an unusual C‐terminal extension consisting of the amino acids glycine, alanine and leucine. This extension results from the mutation of a stop codon into a codon for glycine. The unusual C‐terminal extensions do not seem to interfere with the access of thyroxine to its binding site in the central channel of transthyretin. |
doi_str_mv | 10.1111/j.1432-1033.1995.0977g.x |
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Transthyretin could be identified in medium from in vitro pig choroid plexus incubations by size and number of subunits and a very high rate of synthesis and secretion. Its electrophoretic mobility was intermediate between that of thyroxine‐binding globulin and albumin. It bound thyroxine, retinol‐binding protein, anti‐(rat transthyretin) antibodies and behaved similarly to transthyretins from other vertebrate species when plasma was extracted with phenol. Inhibition experiments with the synthetic flavonoid F 21388, analysing the binding of thyroxine, suggested that transthyretin is not a major thyroxine carrier in the bloodstream of pigs.
Cloning and sequencing of transthyretin cDNA from both choroid plexus and liver showed that the same transthyretin mRNA is expressed in pig choroid plexus and liver. The amino acid sequence derived from the nucleotide sequence revealed that pig transthyretin differs from the transthyretins of all other studied vertebrate species by an unusual C‐terminal extension consisting of the amino acids glycine, alanine and leucine. This extension results from the mutation of a stop codon into a codon for glycine. The unusual C‐terminal extensions do not seem to interfere with the access of thyroxine to its binding site in the central channel of transthyretin.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1995.0977g.x</identifier><identifier>PMID: 7601162</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Choroid Plexus - metabolism ; Chromatography, Affinity ; DNA, Complementary - chemistry ; Molecular Sequence Data ; Pig transthyretin ; pig transthyretin cDNA ; Prealbumin - chemistry ; Prealbumin - genetics ; Prealbumin - metabolism ; Protein Binding ; Protein Conformation ; protein evolution ; Recombinant Proteins - metabolism ; Swine ; Thyroxine - metabolism ; thyroxine binding ; thyroxine transport</subject><ispartof>European journal of biochemistry, 1995-06, Vol.230 (3), p.977-986</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c311G-34dd516d341fcd612a5aa9b3a9bce92206180c465aac3a22e0d59f6293798a8c3</citedby><cites>FETCH-LOGICAL-c311G-34dd516d341fcd612a5aa9b3a9bce92206180c465aac3a22e0d59f6293798a8c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7601162$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Duan, Wei</creatorcontrib><creatorcontrib>Richardson, Samantha J.</creatorcontrib><creatorcontrib>Köhrle, Josef</creatorcontrib><creatorcontrib>Chang, Linus</creatorcontrib><creatorcontrib>Southwell, Bridget R.</creatorcontrib><creatorcontrib>Harms, Paul J.</creatorcontrib><creatorcontrib>Brack, Charlotte M.</creatorcontrib><creatorcontrib>Pettersson, Tom M.</creatorcontrib><creatorcontrib>Schreiber, Gerhard</creatorcontrib><title>Binding of Thyroxine to Pig Transthyretin, its cDNA Structure, and Other Properties</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Thyroxine binding to proteins in pig plasma during electrophoresis was observed in the albumin, but not in the prealbumin and post‐albumin regions.
Transthyretin could be identified in medium from in vitro pig choroid plexus incubations by size and number of subunits and a very high rate of synthesis and secretion. Its electrophoretic mobility was intermediate between that of thyroxine‐binding globulin and albumin. It bound thyroxine, retinol‐binding protein, anti‐(rat transthyretin) antibodies and behaved similarly to transthyretins from other vertebrate species when plasma was extracted with phenol. Inhibition experiments with the synthetic flavonoid F 21388, analysing the binding of thyroxine, suggested that transthyretin is not a major thyroxine carrier in the bloodstream of pigs.
Cloning and sequencing of transthyretin cDNA from both choroid plexus and liver showed that the same transthyretin mRNA is expressed in pig choroid plexus and liver. The amino acid sequence derived from the nucleotide sequence revealed that pig transthyretin differs from the transthyretins of all other studied vertebrate species by an unusual C‐terminal extension consisting of the amino acids glycine, alanine and leucine. This extension results from the mutation of a stop codon into a codon for glycine. The unusual C‐terminal extensions do not seem to interfere with the access of thyroxine to its binding site in the central channel of transthyretin.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Choroid Plexus - metabolism</subject><subject>Chromatography, Affinity</subject><subject>DNA, Complementary - chemistry</subject><subject>Molecular Sequence Data</subject><subject>Pig transthyretin</subject><subject>pig transthyretin cDNA</subject><subject>Prealbumin - chemistry</subject><subject>Prealbumin - genetics</subject><subject>Prealbumin - metabolism</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>protein evolution</subject><subject>Recombinant Proteins - metabolism</subject><subject>Swine</subject><subject>Thyroxine - metabolism</subject><subject>thyroxine binding</subject><subject>thyroxine transport</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkN9LwzAQx4MoOqd_gpAnn2zNJW3avAj-2hSGG2w-h5imW0bXziTF7b-3c8NXPTjuuO_37uCDEAYSQxe3yxgSRiMgjMUgRBoTkWXzeHOEer_CMeoRAklERcrP0Ln3S0IIFzw7RacZJwCc9tD0wdaFree4KfFssXXNxtYGhwZP7BzPnKp96KYm2PoG2-Cxfnq7x9PgWh1aZ26wqgs8Dgvj8MQ1a-OCNf4CnZSq8ubyUPvoffA8e3yJRuPh6-P9KNIMYBixpChS4AVLoNQFB6pSpcQH61IbQSnhkBOd8G6qmaLUkCIVJaeCZSJXuWZ9dL2_u3bNZ2t8kCvrtakqVZum9TLLWMYgSf80As9FzmjSGfO9UbvGe2dKuXZ2pdxWApE78HIpd3zljq_cgZc_4OWmW706_Gg_Vqb4XTyQ7vS7vf5lK7P99105eH6Ydu2QfQNT8JF_</recordid><startdate>19950615</startdate><enddate>19950615</enddate><creator>Duan, Wei</creator><creator>Richardson, Samantha J.</creator><creator>Köhrle, Josef</creator><creator>Chang, Linus</creator><creator>Southwell, Bridget R.</creator><creator>Harms, Paul J.</creator><creator>Brack, Charlotte M.</creator><creator>Pettersson, Tom M.</creator><creator>Schreiber, Gerhard</creator><general>Blackwell Science Ltd</general><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>7QO</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19950615</creationdate><title>Binding of Thyroxine to Pig Transthyretin, its cDNA Structure, and Other Properties</title><author>Duan, Wei ; Richardson, Samantha J. ; Köhrle, Josef ; Chang, Linus ; Southwell, Bridget R. ; Harms, Paul J. ; Brack, Charlotte M. ; Pettersson, Tom M. ; Schreiber, Gerhard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c311G-34dd516d341fcd612a5aa9b3a9bce92206180c465aac3a22e0d59f6293798a8c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Choroid Plexus - metabolism</topic><topic>Chromatography, Affinity</topic><topic>DNA, Complementary - chemistry</topic><topic>Molecular Sequence Data</topic><topic>Pig transthyretin</topic><topic>pig transthyretin cDNA</topic><topic>Prealbumin - chemistry</topic><topic>Prealbumin - genetics</topic><topic>Prealbumin - metabolism</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>protein evolution</topic><topic>Recombinant Proteins - metabolism</topic><topic>Swine</topic><topic>Thyroxine - metabolism</topic><topic>thyroxine binding</topic><topic>thyroxine transport</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Duan, Wei</creatorcontrib><creatorcontrib>Richardson, Samantha J.</creatorcontrib><creatorcontrib>Köhrle, Josef</creatorcontrib><creatorcontrib>Chang, Linus</creatorcontrib><creatorcontrib>Southwell, Bridget R.</creatorcontrib><creatorcontrib>Harms, Paul J.</creatorcontrib><creatorcontrib>Brack, Charlotte M.</creatorcontrib><creatorcontrib>Pettersson, Tom M.</creatorcontrib><creatorcontrib>Schreiber, Gerhard</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Duan, Wei</au><au>Richardson, Samantha J.</au><au>Köhrle, Josef</au><au>Chang, Linus</au><au>Southwell, Bridget R.</au><au>Harms, Paul J.</au><au>Brack, Charlotte M.</au><au>Pettersson, Tom M.</au><au>Schreiber, Gerhard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Binding of Thyroxine to Pig Transthyretin, its cDNA Structure, and Other Properties</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1995-06-15</date><risdate>1995</risdate><volume>230</volume><issue>3</issue><spage>977</spage><epage>986</epage><pages>977-986</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>Thyroxine binding to proteins in pig plasma during electrophoresis was observed in the albumin, but not in the prealbumin and post‐albumin regions.
Transthyretin could be identified in medium from in vitro pig choroid plexus incubations by size and number of subunits and a very high rate of synthesis and secretion. Its electrophoretic mobility was intermediate between that of thyroxine‐binding globulin and albumin. It bound thyroxine, retinol‐binding protein, anti‐(rat transthyretin) antibodies and behaved similarly to transthyretins from other vertebrate species when plasma was extracted with phenol. Inhibition experiments with the synthetic flavonoid F 21388, analysing the binding of thyroxine, suggested that transthyretin is not a major thyroxine carrier in the bloodstream of pigs.
Cloning and sequencing of transthyretin cDNA from both choroid plexus and liver showed that the same transthyretin mRNA is expressed in pig choroid plexus and liver. The amino acid sequence derived from the nucleotide sequence revealed that pig transthyretin differs from the transthyretins of all other studied vertebrate species by an unusual C‐terminal extension consisting of the amino acids glycine, alanine and leucine. This extension results from the mutation of a stop codon into a codon for glycine. The unusual C‐terminal extensions do not seem to interfere with the access of thyroxine to its binding site in the central channel of transthyretin.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>7601162</pmid><doi>10.1111/j.1432-1033.1995.0977g.x</doi><tpages>10</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Base Sequence Choroid Plexus - metabolism Chromatography, Affinity DNA, Complementary - chemistry Molecular Sequence Data Pig transthyretin pig transthyretin cDNA Prealbumin - chemistry Prealbumin - genetics Prealbumin - metabolism Protein Binding Protein Conformation protein evolution Recombinant Proteins - metabolism Swine Thyroxine - metabolism thyroxine binding thyroxine transport |
title | Binding of Thyroxine to Pig Transthyretin, its cDNA Structure, and Other Properties |
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