Characterization of the Goat Lactoferrin cDNA: Assignment of the Relevant Locus to Bovine U12 Synteny Group
Lactoferrin (LTF), which is the major iron-binding protein in milk and physiological fluids, belongs to the transferrin family. We report here the sequence of a caprine LTF cDNA, 2411 bp in length, encoding the pre-protein (709 amino acid residues), Sequence comparisons reveal that structural featur...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1994-09, Vol.203 (2), p.1324-1332 |
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| creator | Leprovost, F. Nocart, M. Guerin, G. Martin, P. |
| description | Lactoferrin (LTF), which is the major iron-binding protein in milk and physiological fluids, belongs to the transferrin family. We report here the sequence of a caprine LTF cDNA, 2411 bp in length, encoding the pre-protein (709 amino acid residues), Sequence comparisons reveal that structural features, including iron-binding sites, cysteine residues involved in disulphide bonds are remarkably conserved between LTF proteins from various species. Of the 5 potential glycosylation sites identified, only one site appears to be conserved between artiodactyls, rodents and humans. Using a somatic cell hybrid panel, the LTF locus was assigned to the bovine U12 syntenic group. This assignment and the localization of the LTF gene on bovine chromosome 22 (BTA 22) by Schwerin et al. (1) using fluorescent in situ hybridization achieves an additional analogy between a synteny group and a chromosome in cuttle. Since serum transferrin (STF) had been previously mapped on BTA 1, in cattle LTF end STF loci are not localized on the same chromosome, conversely to the situation observed in humans (HSA 3) and mice (MMU 9). |
| doi_str_mv | 10.1006/bbrc.1994.2327 |
| format | Article |
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We report here the sequence of a caprine LTF cDNA, 2411 bp in length, encoding the pre-protein (709 amino acid residues), Sequence comparisons reveal that structural features, including iron-binding sites, cysteine residues involved in disulphide bonds are remarkably conserved between LTF proteins from various species. Of the 5 potential glycosylation sites identified, only one site appears to be conserved between artiodactyls, rodents and humans. Using a somatic cell hybrid panel, the LTF locus was assigned to the bovine U12 syntenic group. This assignment and the localization of the LTF gene on bovine chromosome 22 (BTA 22) by Schwerin et al. (1) using fluorescent in situ hybridization achieves an additional analogy between a synteny group and a chromosome in cuttle. Since serum transferrin (STF) had been previously mapped on BTA 1, in cattle LTF end STF loci are not localized on the same chromosome, conversely to the situation observed in humans (HSA 3) and mice (MMU 9).</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.1994.2327</identifier><identifier>PMID: 8093048</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Cattle - genetics ; Chromosome Mapping ; DNA, Complementary - chemistry ; GLICOPROTEINAS ; GLYCOPROTEINE ; Glycosylation ; Goats - genetics ; Humans ; In Situ Hybridization, Fluorescence ; Iron - metabolism ; Lactoferrin - chemistry ; Lactoferrin - genetics ; Lactoferrin - metabolism ; LACTOFERRINAS ; LACTOFERRINE ; LAIT DE CHEVRE ; LECHE DE CABRA ; Life Sciences ; LOCI ; LOCUS ; Molecular Sequence Data ; SECUENCIA NUCLEICA ; Sequence Homology ; SEQUENCE NUCLEIQUE</subject><ispartof>Biochemical and biophysical research communications, 1994-09, Vol.203 (2), p.1324-1332</ispartof><rights>1994 Academic Press</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-2575a05e8370d9ebfc07e955c59d62b078857fbcb7fafb80ff7654a6521313223</citedby><orcidid>0000-0002-0588-5333</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X84723278$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8093048$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02708014$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Leprovost, F.</creatorcontrib><creatorcontrib>Nocart, M.</creatorcontrib><creatorcontrib>Guerin, G.</creatorcontrib><creatorcontrib>Martin, P.</creatorcontrib><title>Characterization of the Goat Lactoferrin cDNA: Assignment of the Relevant Locus to Bovine U12 Synteny Group</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Lactoferrin (LTF), which is the major iron-binding protein in milk and physiological fluids, belongs to the transferrin family. We report here the sequence of a caprine LTF cDNA, 2411 bp in length, encoding the pre-protein (709 amino acid residues), Sequence comparisons reveal that structural features, including iron-binding sites, cysteine residues involved in disulphide bonds are remarkably conserved between LTF proteins from various species. Of the 5 potential glycosylation sites identified, only one site appears to be conserved between artiodactyls, rodents and humans. Using a somatic cell hybrid panel, the LTF locus was assigned to the bovine U12 syntenic group. This assignment and the localization of the LTF gene on bovine chromosome 22 (BTA 22) by Schwerin et al. (1) using fluorescent in situ hybridization achieves an additional analogy between a synteny group and a chromosome in cuttle. Since serum transferrin (STF) had been previously mapped on BTA 1, in cattle LTF end STF loci are not localized on the same chromosome, conversely to the situation observed in humans (HSA 3) and mice (MMU 9).</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Cattle - genetics</subject><subject>Chromosome Mapping</subject><subject>DNA, Complementary - chemistry</subject><subject>GLICOPROTEINAS</subject><subject>GLYCOPROTEINE</subject><subject>Glycosylation</subject><subject>Goats - genetics</subject><subject>Humans</subject><subject>In Situ Hybridization, Fluorescence</subject><subject>Iron - metabolism</subject><subject>Lactoferrin - chemistry</subject><subject>Lactoferrin - genetics</subject><subject>Lactoferrin - metabolism</subject><subject>LACTOFERRINAS</subject><subject>LACTOFERRINE</subject><subject>LAIT DE CHEVRE</subject><subject>LECHE DE CABRA</subject><subject>Life Sciences</subject><subject>LOCI</subject><subject>LOCUS</subject><subject>Molecular Sequence Data</subject><subject>SECUENCIA NUCLEICA</subject><subject>Sequence Homology</subject><subject>SEQUENCE NUCLEIQUE</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kcGL1DAUh4so67h69SAIOQkeOr6kTdN4G0edFYqC64C3kKYvO9GZZjZJB8a_3paOe_MUku_L78H7ZdlLCksKUL1r22CWVMpyyQomHmULChJyRqF8nC1gNHIm6c-n2bMYfwFQWlbyKruqQRZQ1ovs93qngzYJg_ujk_M98ZakHZKN14k0I_EWQ3A9MR-_rt6TVYzurj9gn_6J33GPJz3eG2-GSJInH_zJ9Ui2lJHbc5-wP5NN8MPxefbE6n3EF5fzOtt-_vRjfZM33zZf1qsmN4VkKWdccA0c60JAJ7G1BgRKzg2XXcVaEHXNhW1NK6y2bQ3WioqXuuKMFrRgrLjO3s65O71Xx-AOOpyV107drBo1vQETUAMtT3R038zuMfj7AWNSBxcN7ve6Rz9EJSrBGPBiFJezaIKPMaB9SKagpibU1ISamlBTE-OH15fkoT1g96BfVj_yVzO32it9F1xU21vJqQDJR1jPEMc9nRwGFY3D3mDnApqkOu_-N_cv4qOeIA</recordid><startdate>19940915</startdate><enddate>19940915</enddate><creator>Leprovost, F.</creator><creator>Nocart, M.</creator><creator>Guerin, G.</creator><creator>Martin, P.</creator><general>Elsevier Inc</general><general>Elsevier</general><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>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-0588-5333</orcidid></search><sort><creationdate>19940915</creationdate><title>Characterization of the Goat Lactoferrin cDNA: Assignment of the Relevant Locus to Bovine U12 Synteny Group</title><author>Leprovost, F. ; Nocart, M. ; Guerin, G. ; Martin, P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-2575a05e8370d9ebfc07e955c59d62b078857fbcb7fafb80ff7654a6521313223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Cattle - genetics</topic><topic>Chromosome Mapping</topic><topic>DNA, Complementary - chemistry</topic><topic>GLICOPROTEINAS</topic><topic>GLYCOPROTEINE</topic><topic>Glycosylation</topic><topic>Goats - genetics</topic><topic>Humans</topic><topic>In Situ Hybridization, Fluorescence</topic><topic>Iron - metabolism</topic><topic>Lactoferrin - chemistry</topic><topic>Lactoferrin - genetics</topic><topic>Lactoferrin - metabolism</topic><topic>LACTOFERRINAS</topic><topic>LACTOFERRINE</topic><topic>LAIT DE CHEVRE</topic><topic>LECHE DE CABRA</topic><topic>Life Sciences</topic><topic>LOCI</topic><topic>LOCUS</topic><topic>Molecular Sequence Data</topic><topic>SECUENCIA NUCLEICA</topic><topic>Sequence Homology</topic><topic>SEQUENCE NUCLEIQUE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leprovost, F.</creatorcontrib><creatorcontrib>Nocart, M.</creatorcontrib><creatorcontrib>Guerin, G.</creatorcontrib><creatorcontrib>Martin, P.</creatorcontrib><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>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Leprovost, F.</au><au>Nocart, M.</au><au>Guerin, G.</au><au>Martin, P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of the Goat Lactoferrin cDNA: Assignment of the Relevant Locus to Bovine U12 Synteny Group</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1994-09-15</date><risdate>1994</risdate><volume>203</volume><issue>2</issue><spage>1324</spage><epage>1332</epage><pages>1324-1332</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Lactoferrin (LTF), which is the major iron-binding protein in milk and physiological fluids, belongs to the transferrin family. We report here the sequence of a caprine LTF cDNA, 2411 bp in length, encoding the pre-protein (709 amino acid residues), Sequence comparisons reveal that structural features, including iron-binding sites, cysteine residues involved in disulphide bonds are remarkably conserved between LTF proteins from various species. Of the 5 potential glycosylation sites identified, only one site appears to be conserved between artiodactyls, rodents and humans. Using a somatic cell hybrid panel, the LTF locus was assigned to the bovine U12 syntenic group. This assignment and the localization of the LTF gene on bovine chromosome 22 (BTA 22) by Schwerin et al. (1) using fluorescent in situ hybridization achieves an additional analogy between a synteny group and a chromosome in cuttle. Since serum transferrin (STF) had been previously mapped on BTA 1, in cattle LTF end STF loci are not localized on the same chromosome, conversely to the situation observed in humans (HSA 3) and mice (MMU 9).</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8093048</pmid><doi>10.1006/bbrc.1994.2327</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-0588-5333</orcidid></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1994-09, Vol.203 (2), p.1324-1332 |
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| subjects | Amino Acid Sequence Animals Base Sequence Binding Sites Cattle - genetics Chromosome Mapping DNA, Complementary - chemistry GLICOPROTEINAS GLYCOPROTEINE Glycosylation Goats - genetics Humans In Situ Hybridization, Fluorescence Iron - metabolism Lactoferrin - chemistry Lactoferrin - genetics Lactoferrin - metabolism LACTOFERRINAS LACTOFERRINE LAIT DE CHEVRE LECHE DE CABRA Life Sciences LOCI LOCUS Molecular Sequence Data SECUENCIA NUCLEICA Sequence Homology SEQUENCE NUCLEIQUE |
| title | Characterization of the Goat Lactoferrin cDNA: Assignment of the Relevant Locus to Bovine U12 Synteny Group |
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