Purification and characterization of transforming growth factor-beta 2.3 and -beta 1.2 heterodimers from bovine bone
A unique form of transforming growth factor-beta (TGF-beta), TGF-beta 2.3 heterodimer, has been purified from bovine bone extract. TGF-beta 2.3 migrated as a single 25-kDa band by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, whereas under reducing conditions it migrated as a 12.5 kDa b...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-02, Vol.267 (4), p.2325-2328 |
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| creator | Ogawa, Y Schmidt, D K Dasch, J R Chang, R J Glaser, C B |
| description | A unique form of transforming growth factor-beta (TGF-beta), TGF-beta 2.3 heterodimer, has been purified from bovine bone extract. TGF-beta 2.3 migrated as a single 25-kDa band by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, whereas under reducing conditions it migrated as a 12.5 kDa band. The TGF-beta 2.3 reacted positively with anti-TGF-beta 2 and anti-TGF-beta 3 antibodies on immunoblots. Equal levels of TGF-beta 2 and TGF-beta 3 sequences were detected by N-terminal sequencing. TGF-beta 2.3 eluted as a single sharp peak by reverse-phase high performance liquid chromatography. However, prior reduction of the protein with dithiothreitol resulted in the protein eluting in two peaks, one containing predominantly TGF-beta 3 and the other containing predominantly TGF-beta 2. TGF-beta 2.3 inhibited proliferation of mink lung epithelial cells and promoted the formation of colonies of normal rat kidney fibroblasts in culture with specific biological activity similar to those of TGF-beta 1 and TGF-beta 2. These results demonstrate that the protein is TGF-beta 2.3 heterodimer, consisting of one polypeptide chain each of TGF-beta 2 and TGF-beta 3 linked by one or more disulfide bonds. In addition, TGF-beta 1.2 heterodimer, previously found only in porcine platelets, has also been purified from bovine bone extract. |
| doi_str_mv | 10.1016/S0021-9258(18)45881-4 |
| format | Article |
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TGF-beta 2.3 migrated as a single 25-kDa band by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, whereas under reducing conditions it migrated as a 12.5 kDa band. The TGF-beta 2.3 reacted positively with anti-TGF-beta 2 and anti-TGF-beta 3 antibodies on immunoblots. Equal levels of TGF-beta 2 and TGF-beta 3 sequences were detected by N-terminal sequencing. TGF-beta 2.3 eluted as a single sharp peak by reverse-phase high performance liquid chromatography. However, prior reduction of the protein with dithiothreitol resulted in the protein eluting in two peaks, one containing predominantly TGF-beta 3 and the other containing predominantly TGF-beta 2. TGF-beta 2.3 inhibited proliferation of mink lung epithelial cells and promoted the formation of colonies of normal rat kidney fibroblasts in culture with specific biological activity similar to those of TGF-beta 1 and TGF-beta 2. These results demonstrate that the protein is TGF-beta 2.3 heterodimer, consisting of one polypeptide chain each of TGF-beta 2 and TGF-beta 3 linked by one or more disulfide bonds. In addition, TGF-beta 1.2 heterodimer, previously found only in porcine platelets, has also been purified from bovine bone extract.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)45881-4</identifier><identifier>PMID: 1733936</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Blotting, Western ; bone ; Bone and Bones - chemistry ; BOVIN ; Cattle ; Cells, Cultured ; Chromatography, High Pressure Liquid ; Electrophoresis, Polyacrylamide Gel ; GANADO BOVINO ; HUESOS ; Mink ; Molecular Sequence Data ; PEPTIDE ; PEPTIDOS ; PROTEINAS ; PROTEINE ; PURIFICACION ; PURIFICATION ; Rats ; TECHNIQUE IMMUNOENZYMATIQUE ; TECHNIQUE IMMUNOLOGIQUE ; TECNICAS INMUNOENZIMATICAS ; TECNICAS INMUNOLOGICAS ; Transforming Growth Factor beta - chemistry ; Transforming Growth Factor beta - isolation & purification ; Transforming Growth Factor beta - metabolism</subject><ispartof>The Journal of biological chemistry, 1992-02, Vol.267 (4), p.2325-2328</ispartof><rights>1992 © 1992 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3314-4009138d77739bb8d07893b97092a3b65b44d802a403d71584364321465b6ac73</citedby><cites>FETCH-LOGICAL-c3314-4009138d77739bb8d07893b97092a3b65b44d802a403d71584364321465b6ac73</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/1733936$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ogawa, Y</creatorcontrib><creatorcontrib>Schmidt, D K</creatorcontrib><creatorcontrib>Dasch, J R</creatorcontrib><creatorcontrib>Chang, R J</creatorcontrib><creatorcontrib>Glaser, C B</creatorcontrib><title>Purification and characterization of transforming growth factor-beta 2.3 and -beta 1.2 heterodimers from bovine bone</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A unique form of transforming growth factor-beta (TGF-beta), TGF-beta 2.3 heterodimer, has been purified from bovine bone extract. TGF-beta 2.3 migrated as a single 25-kDa band by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, whereas under reducing conditions it migrated as a 12.5 kDa band. The TGF-beta 2.3 reacted positively with anti-TGF-beta 2 and anti-TGF-beta 3 antibodies on immunoblots. Equal levels of TGF-beta 2 and TGF-beta 3 sequences were detected by N-terminal sequencing. TGF-beta 2.3 eluted as a single sharp peak by reverse-phase high performance liquid chromatography. However, prior reduction of the protein with dithiothreitol resulted in the protein eluting in two peaks, one containing predominantly TGF-beta 3 and the other containing predominantly TGF-beta 2. TGF-beta 2.3 inhibited proliferation of mink lung epithelial cells and promoted the formation of colonies of normal rat kidney fibroblasts in culture with specific biological activity similar to those of TGF-beta 1 and TGF-beta 2. These results demonstrate that the protein is TGF-beta 2.3 heterodimer, consisting of one polypeptide chain each of TGF-beta 2 and TGF-beta 3 linked by one or more disulfide bonds. In addition, TGF-beta 1.2 heterodimer, previously found only in porcine platelets, has also been purified from bovine bone extract.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Blotting, Western</subject><subject>bone</subject><subject>Bone and Bones - chemistry</subject><subject>BOVIN</subject><subject>Cattle</subject><subject>Cells, Cultured</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>GANADO BOVINO</subject><subject>HUESOS</subject><subject>Mink</subject><subject>Molecular Sequence Data</subject><subject>PEPTIDE</subject><subject>PEPTIDOS</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>Rats</subject><subject>TECHNIQUE IMMUNOENZYMATIQUE</subject><subject>TECHNIQUE IMMUNOLOGIQUE</subject><subject>TECNICAS INMUNOENZIMATICAS</subject><subject>TECNICAS INMUNOLOGICAS</subject><subject>Transforming Growth Factor beta - chemistry</subject><subject>Transforming Growth Factor beta - isolation & purification</subject><subject>Transforming Growth Factor beta - metabolism</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>eNqFkU9rFTEUxYNY6mv1CwiF4EJ0Mc_cJDNJVkWK1UJBoRbchfybN5E3k5rMa9FP3_RNsctmc0nO754b7kHoBMgaCHSfrgih0Cjayg8gP_JWSmj4C7QCIlnDWvj1Eq3-I6_QUSm_ST1cwSE6BMGYYt0KzT92OfbRmTmmCZvJYzeYbNwccvy3PKYez9lMpU95jNMGb3K6mwfcVyjlxobZYLpm-97lBmuKh1Adko9jyAX3OY3Ypts4hVqm8Bod9GZbwpvHeoyuz7_8PPvWXH7_enH2-bJxjAFvOCEKmPRCCKaslZ4IqZhVgihqmO1ay7mXhBpOmBfQSs46zijwqnTGCXaM3i--Nzn92YUy6zEWF7ZbM4W0K1pQoajs5LMgdEAlBahgu4Aup1Jy6PVNjqPJfzUQ_RCL3seiH3auQep9LJrXvpPHATs7Bv_UteRQ9XeLPsTNcBdz0DYmN4RR005orimjbYXeLlBvkjabHIu-vlIgFQCt4ukihrrQ2xiyLi6GyQVf3dysfYrP_PEen06uNw</recordid><startdate>19920205</startdate><enddate>19920205</enddate><creator>Ogawa, Y</creator><creator>Schmidt, D K</creator><creator>Dasch, J R</creator><creator>Chang, R J</creator><creator>Glaser, C B</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>7QL</scope><scope>7QP</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19920205</creationdate><title>Purification and characterization of transforming growth factor-beta 2.3 and -beta 1.2 heterodimers from bovine bone</title><author>Ogawa, Y ; Schmidt, D K ; Dasch, J R ; Chang, R J ; Glaser, C B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3314-4009138d77739bb8d07893b97092a3b65b44d802a403d71584364321465b6ac73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Blotting, Western</topic><topic>bone</topic><topic>Bone and Bones - chemistry</topic><topic>BOVIN</topic><topic>Cattle</topic><topic>Cells, Cultured</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>GANADO BOVINO</topic><topic>HUESOS</topic><topic>Mink</topic><topic>Molecular Sequence Data</topic><topic>PEPTIDE</topic><topic>PEPTIDOS</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>Rats</topic><topic>TECHNIQUE IMMUNOENZYMATIQUE</topic><topic>TECHNIQUE IMMUNOLOGIQUE</topic><topic>TECNICAS INMUNOENZIMATICAS</topic><topic>TECNICAS INMUNOLOGICAS</topic><topic>Transforming Growth Factor beta - chemistry</topic><topic>Transforming Growth Factor beta - isolation & purification</topic><topic>Transforming Growth Factor beta - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ogawa, Y</creatorcontrib><creatorcontrib>Schmidt, D K</creatorcontrib><creatorcontrib>Dasch, J R</creatorcontrib><creatorcontrib>Chang, R J</creatorcontrib><creatorcontrib>Glaser, C B</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</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>Ogawa, Y</au><au>Schmidt, D K</au><au>Dasch, J R</au><au>Chang, R J</au><au>Glaser, C B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of transforming growth factor-beta 2.3 and -beta 1.2 heterodimers from bovine bone</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-02-05</date><risdate>1992</risdate><volume>267</volume><issue>4</issue><spage>2325</spage><epage>2328</epage><pages>2325-2328</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>A unique form of transforming growth factor-beta (TGF-beta), TGF-beta 2.3 heterodimer, has been purified from bovine bone extract. TGF-beta 2.3 migrated as a single 25-kDa band by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, whereas under reducing conditions it migrated as a 12.5 kDa band. The TGF-beta 2.3 reacted positively with anti-TGF-beta 2 and anti-TGF-beta 3 antibodies on immunoblots. Equal levels of TGF-beta 2 and TGF-beta 3 sequences were detected by N-terminal sequencing. TGF-beta 2.3 eluted as a single sharp peak by reverse-phase high performance liquid chromatography. However, prior reduction of the protein with dithiothreitol resulted in the protein eluting in two peaks, one containing predominantly TGF-beta 3 and the other containing predominantly TGF-beta 2. TGF-beta 2.3 inhibited proliferation of mink lung epithelial cells and promoted the formation of colonies of normal rat kidney fibroblasts in culture with specific biological activity similar to those of TGF-beta 1 and TGF-beta 2. These results demonstrate that the protein is TGF-beta 2.3 heterodimer, consisting of one polypeptide chain each of TGF-beta 2 and TGF-beta 3 linked by one or more disulfide bonds. In addition, TGF-beta 1.2 heterodimer, previously found only in porcine platelets, has also been purified from bovine bone extract.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>1733936</pmid><doi>10.1016/S0021-9258(18)45881-4</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Blotting, Western bone Bone and Bones - chemistry BOVIN Cattle Cells, Cultured Chromatography, High Pressure Liquid Electrophoresis, Polyacrylamide Gel GANADO BOVINO HUESOS Mink Molecular Sequence Data PEPTIDE PEPTIDOS PROTEINAS PROTEINE PURIFICACION PURIFICATION Rats TECHNIQUE IMMUNOENZYMATIQUE TECHNIQUE IMMUNOLOGIQUE TECNICAS INMUNOENZIMATICAS TECNICAS INMUNOLOGICAS Transforming Growth Factor beta - chemistry Transforming Growth Factor beta - isolation & purification Transforming Growth Factor beta - metabolism |
| title | Purification and characterization of transforming growth factor-beta 2.3 and -beta 1.2 heterodimers from bovine bone |
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