Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II
Identifieur interne : 003311 ( Main/Exploration ); précédent : 003310; suivant : 003312Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II
Auteurs : Hiroshi Murakami [États-Unis] ; Gregory P. Marelich [États-Unis] ; Jeffrey H. Grubb [États-Unis] ; John W. Kyle [États-Unis] ; William S. Sly [États-Unis]Source :
- Genomics [ 0888-7543 ] ; 1987.
English descriptors
- Teeft :
- Acad, Academic press, Active site residues, Active sites, Amino, Amino acid residues, Amino acid sequence, Amino acids, Anhydrase, Anhydrases, Carbonic, Carbonic anhydrase, Carbonic anhydrase isozymes, Carbonic anhydrases, Cdna, Cdna clone, Cells transfected, Cerebral calcification, Clone, Ecori, Ecori site, Genomic clone, Homology, Human carbonic anhydrase, Human kidney, Isozymes, Murakami, Nucleic acids, Nucleotide, Nucleotide position, Nucleotide positions, Nucleotide sequence, Nucleotide sequences, Sequencing, Synthetic oligonucleotide, Tashian, Transfected, Transfected cells, Venta, Xhm3.
Abstract
Abstract: A cDNA clone for human carbonic anhydrase (CA) II was isolated from a kidney λgt10 library. Expression of the cDNA insert in Cos-7 cells produced an immunoprecipitable product and enzymatically active carbonic anhydrase. The cDNA insert is 1551 bp in length and contains an open reading frame which encodes a 260-amino-acid polypeptide. The deduced amino acid sequence is identical to that reported for human CA II. The protein coding region of this cDNA for human CA II shows 81 and 70% nucleotide identity with cDNAs for CA II from mouse and chick, respectively. Even the long 3′-untranslated region of the cDNA for human CA II (703 bp) is 64 and 42% identical to those of CA II from mouse and chick, showing remarkable conservation of the CA II cDNAs in amniotes. The protein coding region of the human CA II cDNA is 64 and 65% identical with those of human CA I and CA III, which are thought to have arisen from a common precursor by gene duplication.
Url:
DOI: 10.1016/0888-7543(87)90008-5
Affiliations:
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A. Doisy Department of Biochemistry, St. Louis University School of Medicine, St. Louis</wicri:cityArea></affiliation></author><author><name sortKey="Marelich, Gregory P" sort="Marelich, Gregory P" uniqKey="Marelich G" first="Gregory P." last="Marelich">Gregory P. Marelich</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Missouri (État)</region></placeName><wicri:cityArea>E. A. Doisy Department of Biochemistry, St. Louis University School of Medicine, St. Louis</wicri:cityArea></affiliation></author><author><name sortKey="Grubb, Jeffrey H" sort="Grubb, Jeffrey H" uniqKey="Grubb J" first="Jeffrey H." last="Grubb">Jeffrey H. Grubb</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Missouri (État)</region></placeName><wicri:cityArea>E. A. Doisy Department of Biochemistry, St. Louis University School of Medicine, St. Louis</wicri:cityArea></affiliation></author><author><name sortKey="Kyle, John W" sort="Kyle, John W" uniqKey="Kyle J" first="John W." last="Kyle">John W. Kyle</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Missouri (État)</region></placeName><wicri:cityArea>E. A. Doisy Department of Biochemistry, St. Louis University School of Medicine, St. Louis</wicri:cityArea></affiliation></author><author><name sortKey="Sly, William S" sort="Sly, William S" uniqKey="Sly W" first="William S." last="Sly">William S. Sly</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Missouri (État)</region></placeName><wicri:cityArea>E. A. Doisy Department of Biochemistry, St. Louis University School of Medicine, St. Louis</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Genomics</title><title level="j" type="abbrev">YGENO</title><idno type="ISSN">0888-7543</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987">1987</date><biblScope unit="volume">1</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="159">159</biblScope><biblScope unit="page" to="166">166</biblScope></imprint><idno type="ISSN">0888-7543</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0888-7543</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Academic press</term><term>Active site residues</term><term>Active sites</term><term>Amino</term><term>Amino acid residues</term><term>Amino acid sequence</term><term>Amino acids</term><term>Anhydrase</term><term>Anhydrases</term><term>Carbonic</term><term>Carbonic anhydrase</term><term>Carbonic anhydrase isozymes</term><term>Carbonic anhydrases</term><term>Cdna</term><term>Cdna clone</term><term>Cells transfected</term><term>Cerebral calcification</term><term>Clone</term><term>Ecori</term><term>Ecori site</term><term>Genomic clone</term><term>Homology</term><term>Human carbonic anhydrase</term><term>Human kidney</term><term>Isozymes</term><term>Murakami</term><term>Nucleic acids</term><term>Nucleotide</term><term>Nucleotide position</term><term>Nucleotide positions</term><term>Nucleotide sequence</term><term>Nucleotide sequences</term><term>Sequencing</term><term>Synthetic oligonucleotide</term><term>Tashian</term><term>Transfected</term><term>Transfected cells</term><term>Venta</term><term>Xhm3</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: A cDNA clone for human carbonic anhydrase (CA) II was isolated from a kidney λgt10 library. Expression of the cDNA insert in Cos-7 cells produced an immunoprecipitable product and enzymatically active carbonic anhydrase. The cDNA insert is 1551 bp in length and contains an open reading frame which encodes a 260-amino-acid polypeptide. The deduced amino acid sequence is identical to that reported for human CA II. The protein coding region of this cDNA for human CA II shows 81 and 70% nucleotide identity with cDNAs for CA II from mouse and chick, respectively. Even the long 3′-untranslated region of the cDNA for human CA II (703 bp) is 64 and 42% identical to those of CA II from mouse and chick, showing remarkable conservation of the CA II cDNAs in amniotes. The protein coding region of the human CA II cDNA is 64 and 65% identical with those of human CA I and CA III, which are thought to have arisen from a common precursor by gene duplication.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Missouri (État)</li></region></list><tree><country name="États-Unis"><region name="Missouri (État)"><name sortKey="Murakami, Hiroshi" sort="Murakami, Hiroshi" uniqKey="Murakami H" first="Hiroshi" last="Murakami">Hiroshi Murakami</name></region><name sortKey="Grubb, Jeffrey H" sort="Grubb, Jeffrey H" uniqKey="Grubb J" first="Jeffrey H." last="Grubb">Jeffrey H. Grubb</name><name sortKey="Kyle, John W" sort="Kyle, John W" uniqKey="Kyle J" first="John W." last="Kyle">John W. Kyle</name><name sortKey="Marelich, Gregory P" sort="Marelich, Gregory P" uniqKey="Marelich G" first="Gregory P." last="Marelich">Gregory P. Marelich</name><name sortKey="Sly, William S" sort="Sly, William S" uniqKey="Sly W" first="William S." last="Sly">William S. Sly</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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