Cloning and sequence analysis of cDNA for bovine carboxypeptidase E
Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in the biosynthesis of enkephalin in bovine adrenal chromaffin granules 1 . A similar enzyme is present in many brain regions 1,2 and in purified secretory granules from rat pituitary 3 and...
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| Veröffentlicht in: | Nature (London) 1986-10, Vol.323 (6087), p.461-464 |
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| creator | Fricker, Lloyd D Evans, Chris J Esch, Fred S Herbert, Edward |
| description | Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in the biosynthesis of enkephalin in bovine adrenal chromaffin granules
1
. A similar enzyme is present in many brain regions
1,2
and in purified secretory granules from rat pituitary
3
and rat insulinoma
4
. Within the secretory granules, carboxypeptidase E (CPE) activity is found in both a soluble and a membrane-bound form
1
, which differ slightly in relative molecular mass (
M
r
)
5
. Here, to investigate whether the CPE activities in the various tissues are produced from a single gene, purified CPE was partially sequenced and oligonucleotide probes were used to isolate a clone encoding CPE from a bovine pituitary complementary DNA library. This cDNA hybridizes to bovine pituitary poly(A)
+
RNAs of approximately 3.3, 2.6 and 2.1 kilobases (kb), with the 3.3-kb messenger RNA the predominant species. The predicted amino-acid sequence of the cDNA clone contains the partially determined sequences of CPE, several pairs of basic amino acids and displays some homology with both carboxypeptidases A and B. Restriction analysis of bovine genomic DNA suggests only one gene for CPE. This is consistent with a broad role for CPE in the biosynthesis of many neuropeptides. |
| doi_str_mv | 10.1038/323461a0 |
| format | Article |
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1
. A similar enzyme is present in many brain regions
1,2
and in purified secretory granules from rat pituitary
3
and rat insulinoma
4
. Within the secretory granules, carboxypeptidase E (CPE) activity is found in both a soluble and a membrane-bound form
1
, which differ slightly in relative molecular mass (
M
r
)
5
. Here, to investigate whether the CPE activities in the various tissues are produced from a single gene, purified CPE was partially sequenced and oligonucleotide probes were used to isolate a clone encoding CPE from a bovine pituitary complementary DNA library. This cDNA hybridizes to bovine pituitary poly(A)
+
RNAs of approximately 3.3, 2.6 and 2.1 kilobases (kb), with the 3.3-kb messenger RNA the predominant species. The predicted amino-acid sequence of the cDNA clone contains the partially determined sequences of CPE, several pairs of basic amino acids and displays some homology with both carboxypeptidases A and B. Restriction analysis of bovine genomic DNA suggests only one gene for CPE. This is consistent with a broad role for CPE in the biosynthesis of many neuropeptides.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/323461a0</identifier><identifier>PMID: 3020433</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Biological and medical sciences ; Biotechnology ; carboxypeptidase E ; Carboxypeptidase H ; Carboxypeptidases - genetics ; Cattle ; cDNA ; Cloning, Molecular ; DNA ; DNA Restriction Enzymes ; Fundamental and applied biological sciences. Psychology ; genes ; Genes. Genome ; Genetic engineering ; Genetic technics ; Humanities and Social Sciences ; letter ; Methods. Procedures. Technologies ; Molecular and cellular biology ; Molecular genetics ; multidisciplinary ; Nucleic Acid Hybridization ; nucleotide sequence ; Pituitary Gland - metabolism ; restriction endonuclease mapping ; Science ; Science (multidisciplinary) ; Sequence Homology, Nucleic Acid ; Synthetic digonucleotides and genes. Sequencing</subject><ispartof>Nature (London), 1986-10, Vol.323 (6087), p.461-464</ispartof><rights>Springer Nature Limited 1986</rights><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c429t-7318c6c96450b7872f5e2471b981c9ca0d591f8715c2e002e294095e128d1d9e3</citedby><cites>FETCH-LOGICAL-c429t-7318c6c96450b7872f5e2471b981c9ca0d591f8715c2e002e294095e128d1d9e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2727,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7973309$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3020433$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fricker, Lloyd D</creatorcontrib><creatorcontrib>Evans, Chris J</creatorcontrib><creatorcontrib>Esch, Fred S</creatorcontrib><creatorcontrib>Herbert, Edward</creatorcontrib><title>Cloning and sequence analysis of cDNA for bovine carboxypeptidase E</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in the biosynthesis of enkephalin in bovine adrenal chromaffin granules
1
. A similar enzyme is present in many brain regions
1,2
and in purified secretory granules from rat pituitary
3
and rat insulinoma
4
. Within the secretory granules, carboxypeptidase E (CPE) activity is found in both a soluble and a membrane-bound form
1
, which differ slightly in relative molecular mass (
M
r
)
5
. Here, to investigate whether the CPE activities in the various tissues are produced from a single gene, purified CPE was partially sequenced and oligonucleotide probes were used to isolate a clone encoding CPE from a bovine pituitary complementary DNA library. This cDNA hybridizes to bovine pituitary poly(A)
+
RNAs of approximately 3.3, 2.6 and 2.1 kilobases (kb), with the 3.3-kb messenger RNA the predominant species. The predicted amino-acid sequence of the cDNA clone contains the partially determined sequences of CPE, several pairs of basic amino acids and displays some homology with both carboxypeptidases A and B. Restriction analysis of bovine genomic DNA suggests only one gene for CPE. This is consistent with a broad role for CPE in the biosynthesis of many neuropeptides.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>carboxypeptidase E</subject><subject>Carboxypeptidase H</subject><subject>Carboxypeptidases - genetics</subject><subject>Cattle</subject><subject>cDNA</subject><subject>Cloning, Molecular</subject><subject>DNA</subject><subject>DNA Restriction Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Genes. Genome</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Humanities and Social Sciences</subject><subject>letter</subject><subject>Methods. Procedures. Technologies</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>multidisciplinary</subject><subject>Nucleic Acid Hybridization</subject><subject>nucleotide sequence</subject><subject>Pituitary Gland - metabolism</subject><subject>restriction endonuclease mapping</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Synthetic digonucleotides and genes. Sequencing</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0MtKxDAUBuAgyjhewBdQuhDRRfXk0iZZyniFQTe6Lml6KpVOMiZTcd7eyIy6EVyF8H-cc_gJOaBwToGrC864KKmBDTKmQpa5KJXcJGMApnJQvNwmOzG-AkBBpRiREQcGgvMxmUx67zr3khnXZBHfBnQW08f0y9jFzLeZvXq4zFofstq_dw4za0LtP5ZznC-6xkTMrvfIVmv6iPvrd5c831w_Te7y6ePt_eRymlvB9CKXnCpbWl2KAmqpJGsLZELSWitqtTXQFJq2StLCMkyXI9MCdIGUqYY2GvkuOVnNnQefDo2LatZFi31vHPohVlJCWTLK_4VUFEoKyRI8XUEbfIwB22oeupkJy4pC9VVs9V1soofrmUM9w-YHrptM-fE6N9Gavg3G2S7-MKkl56ATO1uxmBL3gqF69UNIdce_Vh6trDOLIeDvym_wCQohk8M</recordid><startdate>19861002</startdate><enddate>19861002</enddate><creator>Fricker, Lloyd D</creator><creator>Evans, Chris J</creator><creator>Esch, Fred S</creator><creator>Herbert, Edward</creator><general>Nature Publishing Group UK</general><general>Nature Publishing</general><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>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19861002</creationdate><title>Cloning and sequence analysis of cDNA for bovine carboxypeptidase E</title><author>Fricker, Lloyd D ; Evans, Chris J ; Esch, Fred S ; Herbert, Edward</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c429t-7318c6c96450b7872f5e2471b981c9ca0d591f8715c2e002e294095e128d1d9e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>carboxypeptidase E</topic><topic>Carboxypeptidase H</topic><topic>Carboxypeptidases - genetics</topic><topic>Cattle</topic><topic>cDNA</topic><topic>Cloning, Molecular</topic><topic>DNA</topic><topic>DNA Restriction Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Genes. Genome</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>Humanities and Social Sciences</topic><topic>letter</topic><topic>Methods. Procedures. Technologies</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>multidisciplinary</topic><topic>Nucleic Acid Hybridization</topic><topic>nucleotide sequence</topic><topic>Pituitary Gland - metabolism</topic><topic>restriction endonuclease mapping</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Synthetic digonucleotides and genes. Sequencing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fricker, Lloyd D</creatorcontrib><creatorcontrib>Evans, Chris J</creatorcontrib><creatorcontrib>Esch, Fred S</creatorcontrib><creatorcontrib>Herbert, Edward</creatorcontrib><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>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fricker, Lloyd D</au><au>Evans, Chris J</au><au>Esch, Fred S</au><au>Herbert, Edward</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and sequence analysis of cDNA for bovine carboxypeptidase E</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1986-10-02</date><risdate>1986</risdate><volume>323</volume><issue>6087</issue><spage>461</spage><epage>464</epage><pages>461-464</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in the biosynthesis of enkephalin in bovine adrenal chromaffin granules
1
. A similar enzyme is present in many brain regions
1,2
and in purified secretory granules from rat pituitary
3
and rat insulinoma
4
. Within the secretory granules, carboxypeptidase E (CPE) activity is found in both a soluble and a membrane-bound form
1
, which differ slightly in relative molecular mass (
M
r
)
5
. Here, to investigate whether the CPE activities in the various tissues are produced from a single gene, purified CPE was partially sequenced and oligonucleotide probes were used to isolate a clone encoding CPE from a bovine pituitary complementary DNA library. This cDNA hybridizes to bovine pituitary poly(A)
+
RNAs of approximately 3.3, 2.6 and 2.1 kilobases (kb), with the 3.3-kb messenger RNA the predominant species. The predicted amino-acid sequence of the cDNA clone contains the partially determined sequences of CPE, several pairs of basic amino acids and displays some homology with both carboxypeptidases A and B. Restriction analysis of bovine genomic DNA suggests only one gene for CPE. This is consistent with a broad role for CPE in the biosynthesis of many neuropeptides.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>3020433</pmid><doi>10.1038/323461a0</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Base Sequence Biological and medical sciences Biotechnology carboxypeptidase E Carboxypeptidase H Carboxypeptidases - genetics Cattle cDNA Cloning, Molecular DNA DNA Restriction Enzymes Fundamental and applied biological sciences. Psychology genes Genes. Genome Genetic engineering Genetic technics Humanities and Social Sciences letter Methods. Procedures. Technologies Molecular and cellular biology Molecular genetics multidisciplinary Nucleic Acid Hybridization nucleotide sequence Pituitary Gland - metabolism restriction endonuclease mapping Science Science (multidisciplinary) Sequence Homology, Nucleic Acid Synthetic digonucleotides and genes. Sequencing |
| title | Cloning and sequence analysis of cDNA for bovine carboxypeptidase E |
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