Cloning of the cDNAs encoding the cellular retinaldehyde-binding protein from bovine and human retina and comparison of the protein structures
A 1173-base pair cDNA encoding bovine cellular retinaldehyde-binding protein (CRALBP) was cloned from a bovine retinal cDNA expression library using as probes both anti-CRALBP polyclonal and monoclonal antibodies. The amino acid sequence deduced from the cDNA corresponds exactly to that determined b...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 1988-12, Vol.263 (35), p.18688-18692 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 18692 |
|---|---|
| container_issue | 35 |
| container_start_page | 18688 |
| container_title | The Journal of biological chemistry |
| container_volume | 263 |
| creator | Crabb, J W Goldflam, S Harris, S E Saari, J C |
| description | A 1173-base pair cDNA encoding bovine cellular retinaldehyde-binding protein (CRALBP) was cloned from a bovine retinal cDNA expression library using as probes both anti-CRALBP polyclonal and monoclonal antibodies. The amino acid sequence deduced from the cDNA corresponds exactly to that determined by direct analysis of NH2-terminally acetylated bovine CRALBP (Crabb, J. W., Johnson, C. M., Carr, S. A., Armes, L. G., and Saari, J. C. (1988) J. Biol. Chem. 263, 18678-18687). Nick-translated bovine CRALBP cDNA probes were then used to clone from a human retinal cDNA library a 1317-base pair cDNA encoding human CRALBP. Bovine and human CRALBP are 92% identical in amino acid sequence and not related to any other known protein sequence. Both the bovine and human proteins contain 316 residues and have calculated molecular weights of 36,378 and 36,347, respectively, exclusive of the NH2-terminal blocking groups. The CRALBP cDNA clones should prove valuable as tools for studying the physiological role of the protein in vision and visual disorders. |
| doi_str_mv | 10.1016/S0021-9258(18)37339-3 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_78567805</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925818373393</els_id><sourcerecordid>78567805</sourcerecordid><originalsourceid>FETCH-LOGICAL-c562t-d83b87c90ac2880b5103dd445cf732871c16f364acd8262727165610604a53743</originalsourceid><addsrcrecordid>eNqFkctu1TAQhi0EKofCI1TKAiFYBHyJL1mh6nCVKlgAEjvLsSeNUWIf7KSoL8Ezk-Skh2W9sTTz_fOP_SN0QfBrgol48w1jSsqacvWSqFdMMlaX7AHaEaxYyTj5-RDtTshj9CTnX3g-VU3O0BkjteI136G_-z4GH66L2BZjB4V99-UyFxBsdEt1LUHfT71JRYLRB9M76G4dlI0PK3JIcQQfijbFoWjijQ9QmOCKbhpM2DRrwcbhYJLPMdyZ3UnzmCY7TgnyU_SoNX2GZ9t9jn58eP99_6m8-vrx8_7yqrRc0LF0ijVK2hobS5XCDSeYOVdV3LaSUSWJJaJlojLWKSqopJIILggWuDKcyYqdoxfHufMKvyfIox58Xh5qAsQpa6m4kArze0HCscSCLxP5EbQp5pyg1YfkB5NuNcF6CUyvgeklDU2UXgPTbNZdbAZTM4A7qbaE5v7zrW-yNX2bTLA-nzBJsago-Y91_rr74xPoxkfbwaCpYJrx2VIoNWNvjxjMn3vjIels_Zw2uFliR-2iv2fff1y7vpY</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15070654</pqid></control><display><type>article</type><title>Cloning of the cDNAs encoding the cellular retinaldehyde-binding protein from bovine and human retina and comparison of the protein structures</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Crabb, J W ; Goldflam, S ; Harris, S E ; Saari, J C</creator><creatorcontrib>Crabb, J W ; Goldflam, S ; Harris, S E ; Saari, J C</creatorcontrib><description>A 1173-base pair cDNA encoding bovine cellular retinaldehyde-binding protein (CRALBP) was cloned from a bovine retinal cDNA expression library using as probes both anti-CRALBP polyclonal and monoclonal antibodies. The amino acid sequence deduced from the cDNA corresponds exactly to that determined by direct analysis of NH2-terminally acetylated bovine CRALBP (Crabb, J. W., Johnson, C. M., Carr, S. A., Armes, L. G., and Saari, J. C. (1988) J. Biol. Chem. 263, 18678-18687). Nick-translated bovine CRALBP cDNA probes were then used to clone from a human retinal cDNA library a 1317-base pair cDNA encoding human CRALBP. Bovine and human CRALBP are 92% identical in amino acid sequence and not related to any other known protein sequence. Both the bovine and human proteins contain 316 residues and have calculated molecular weights of 36,378 and 36,347, respectively, exclusive of the NH2-terminal blocking groups. The CRALBP cDNA clones should prove valuable as tools for studying the physiological role of the protein in vision and visual disorders.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)37339-3</identifier><identifier>PMID: 3198595</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Animals ; Biological and medical sciences ; Biotechnology ; Carrier Proteins - genetics ; Cattle ; Cloning, Molecular ; DNA - analysis ; Fundamental and applied biological sciences. Psychology ; Genes. Genome ; Genetic engineering ; Genetic technics ; Methods. Procedures. Technologies ; Molecular and cellular biology ; Molecular cloning ; Molecular genetics ; Molecular Sequence Data ; Retina - analysis</subject><ispartof>The Journal of biological chemistry, 1988-12, Vol.263 (35), p.18688-18692</ispartof><rights>1988 © 1988 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c562t-d83b87c90ac2880b5103dd445cf732871c16f364acd8262727165610604a53743</citedby><cites>FETCH-LOGICAL-c562t-d83b87c90ac2880b5103dd445cf732871c16f364acd8262727165610604a53743</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=7206421$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3198595$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Crabb, J W</creatorcontrib><creatorcontrib>Goldflam, S</creatorcontrib><creatorcontrib>Harris, S E</creatorcontrib><creatorcontrib>Saari, J C</creatorcontrib><title>Cloning of the cDNAs encoding the cellular retinaldehyde-binding protein from bovine and human retina and comparison of the protein structures</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A 1173-base pair cDNA encoding bovine cellular retinaldehyde-binding protein (CRALBP) was cloned from a bovine retinal cDNA expression library using as probes both anti-CRALBP polyclonal and monoclonal antibodies. The amino acid sequence deduced from the cDNA corresponds exactly to that determined by direct analysis of NH2-terminally acetylated bovine CRALBP (Crabb, J. W., Johnson, C. M., Carr, S. A., Armes, L. G., and Saari, J. C. (1988) J. Biol. Chem. 263, 18678-18687). Nick-translated bovine CRALBP cDNA probes were then used to clone from a human retinal cDNA library a 1317-base pair cDNA encoding human CRALBP. Bovine and human CRALBP are 92% identical in amino acid sequence and not related to any other known protein sequence. Both the bovine and human proteins contain 316 residues and have calculated molecular weights of 36,378 and 36,347, respectively, exclusive of the NH2-terminal blocking groups. The CRALBP cDNA clones should prove valuable as tools for studying the physiological role of the protein in vision and visual disorders.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Carrier Proteins - genetics</subject><subject>Cattle</subject><subject>Cloning, Molecular</subject><subject>DNA - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes. Genome</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Methods. Procedures. Technologies</subject><subject>Molecular and cellular biology</subject><subject>Molecular cloning</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Retina - analysis</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctu1TAQhi0EKofCI1TKAiFYBHyJL1mh6nCVKlgAEjvLsSeNUWIf7KSoL8Ezk-Skh2W9sTTz_fOP_SN0QfBrgol48w1jSsqacvWSqFdMMlaX7AHaEaxYyTj5-RDtTshj9CTnX3g-VU3O0BkjteI136G_-z4GH66L2BZjB4V99-UyFxBsdEt1LUHfT71JRYLRB9M76G4dlI0PK3JIcQQfijbFoWjijQ9QmOCKbhpM2DRrwcbhYJLPMdyZ3UnzmCY7TgnyU_SoNX2GZ9t9jn58eP99_6m8-vrx8_7yqrRc0LF0ijVK2hobS5XCDSeYOVdV3LaSUSWJJaJlojLWKSqopJIILggWuDKcyYqdoxfHufMKvyfIox58Xh5qAsQpa6m4kArze0HCscSCLxP5EbQp5pyg1YfkB5NuNcF6CUyvgeklDU2UXgPTbNZdbAZTM4A7qbaE5v7zrW-yNX2bTLA-nzBJsago-Y91_rr74xPoxkfbwaCpYJrx2VIoNWNvjxjMn3vjIels_Zw2uFliR-2iv2fff1y7vpY</recordid><startdate>19881215</startdate><enddate>19881215</enddate><creator>Crabb, J W</creator><creator>Goldflam, S</creator><creator>Harris, S E</creator><creator>Saari, J C</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19881215</creationdate><title>Cloning of the cDNAs encoding the cellular retinaldehyde-binding protein from bovine and human retina and comparison of the protein structures</title><author>Crabb, J W ; Goldflam, S ; Harris, S E ; Saari, J C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c562t-d83b87c90ac2880b5103dd445cf732871c16f364acd8262727165610604a53743</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Carrier Proteins - genetics</topic><topic>Cattle</topic><topic>Cloning, Molecular</topic><topic>DNA - analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes. Genome</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>Methods. Procedures. Technologies</topic><topic>Molecular and cellular biology</topic><topic>Molecular cloning</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Retina - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Crabb, J W</creatorcontrib><creatorcontrib>Goldflam, S</creatorcontrib><creatorcontrib>Harris, S E</creatorcontrib><creatorcontrib>Saari, J C</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Crabb, J W</au><au>Goldflam, S</au><au>Harris, S E</au><au>Saari, J C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning of the cDNAs encoding the cellular retinaldehyde-binding protein from bovine and human retina and comparison of the protein structures</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1988-12-15</date><risdate>1988</risdate><volume>263</volume><issue>35</issue><spage>18688</spage><epage>18692</epage><pages>18688-18692</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>A 1173-base pair cDNA encoding bovine cellular retinaldehyde-binding protein (CRALBP) was cloned from a bovine retinal cDNA expression library using as probes both anti-CRALBP polyclonal and monoclonal antibodies. The amino acid sequence deduced from the cDNA corresponds exactly to that determined by direct analysis of NH2-terminally acetylated bovine CRALBP (Crabb, J. W., Johnson, C. M., Carr, S. A., Armes, L. G., and Saari, J. C. (1988) J. Biol. Chem. 263, 18678-18687). Nick-translated bovine CRALBP cDNA probes were then used to clone from a human retinal cDNA library a 1317-base pair cDNA encoding human CRALBP. Bovine and human CRALBP are 92% identical in amino acid sequence and not related to any other known protein sequence. Both the bovine and human proteins contain 316 residues and have calculated molecular weights of 36,378 and 36,347, respectively, exclusive of the NH2-terminal blocking groups. The CRALBP cDNA clones should prove valuable as tools for studying the physiological role of the protein in vision and visual disorders.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>3198595</pmid><doi>10.1016/S0021-9258(18)37339-3</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1988-12, Vol.263 (35), p.18688-18692 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78567805 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Biological and medical sciences Biotechnology Carrier Proteins - genetics Cattle Cloning, Molecular DNA - analysis Fundamental and applied biological sciences. Psychology Genes. Genome Genetic engineering Genetic technics Methods. Procedures. Technologies Molecular and cellular biology Molecular cloning Molecular genetics Molecular Sequence Data Retina - analysis |
| title | Cloning of the cDNAs encoding the cellular retinaldehyde-binding protein from bovine and human retina and comparison of the protein structures |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-26T05%3A32%3A40IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cloning%20of%20the%20cDNAs%20encoding%20the%20cellular%20retinaldehyde-binding%20protein%20from%20bovine%20and%20human%20retina%20and%20comparison%20of%20the%20protein%20structures&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Crabb,%20J%20W&rft.date=1988-12-15&rft.volume=263&rft.issue=35&rft.spage=18688&rft.epage=18692&rft.pages=18688-18692&rft.issn=0021-9258&rft.eissn=1083-351X&rft.coden=JBCHA3&rft_id=info:doi/10.1016/S0021-9258(18)37339-3&rft_dat=%3Cproquest_cross%3E78567805%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15070654&rft_id=info:pmid/3198595&rft_els_id=S0021925818373393&rfr_iscdi=true |