The primary structure of pig liver thioltransferase.
Identifieur interne : 001344 ( Main/Exploration ); précédent : 001343; suivant : 001345The primary structure of pig liver thioltransferase.
Auteurs : Z R Gan ; W W WellsSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1987.
Descripteurs français
- KwdFr :
- MESH :
- analyse : Fragments peptidiques.
- enzymologie : Foie.
- Animaux, Glutarédoxines, Oxidoreductases, Protein-disulfide reductase (glutathione), Spectrométrie de masse, Suidae, Séquence d'acides aminés, Trypsine.
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Peptide Fragments.
- chemical : Glutaredoxins, Oxidoreductases, Protein Disulfide Reductase (Glutathione), Trypsin.
- enzymology : Liver.
- Amino Acid Sequence, Animals, Mass Spectrometry, Swine.
Abstract
The complete amino acid sequence of pig liver thioltransferase has been determined. The homogeneous protein was cleaved by trypsin, chymotrypsin, Staphylococcus aureus V8 protease, and cyanogen bromide. The resulting peptides were purified by reversed-phase high performance liquid chromatography and ion-exchange fast protein liquid chromatography. Sequencing of the fragments was achieved with either automated Edman degradation or fast atom bombardment-mass spectrometry. Pig liver thioltransferase is a single polypeptide with 105 amino acid residues and an acetylated glutamine N terminus. The protein has 2 cysteine pairs with sequences of -Cys-Pro-Phe-Cys- and -Cys-Ile-Gly-Gly-Cys-, the first pair of which (Cys22 and Cys25) is located at the potential active site of the enzyme. The sequence of pig liver thioltransferase displays close homology (82%) with calf thymus glutaredoxin, suggesting that they belong to the same evolutionary family.
PubMed: 3571278
Affiliations:
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Le document en format XML
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The homogeneous protein was cleaved by trypsin, chymotrypsin, Staphylococcus aureus V8 protease, and cyanogen bromide. The resulting peptides were purified by reversed-phase high performance liquid chromatography and ion-exchange fast protein liquid chromatography. Sequencing of the fragments was achieved with either automated Edman degradation or fast atom bombardment-mass spectrometry. Pig liver thioltransferase is a single polypeptide with 105 amino acid residues and an acetylated glutamine N terminus. The protein has 2 cysteine pairs with sequences of -Cys-Pro-Phe-Cys- and -Cys-Ile-Gly-Gly-Cys-, the first pair of which (Cys22 and Cys25) is located at the potential active site of the enzyme. The sequence of pig liver thioltransferase displays close homology (82%) with calf thymus glutaredoxin, suggesting that they belong to the same evolutionary family.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">3571278</PMID><DateCompleted><Year>1987</Year><Month>06</Month><Day>19</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>262</Volume><Issue>14</Issue><PubDate><Year>1987</Year><Month>May</Month><Day>15</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>The primary structure of pig liver thioltransferase.</ArticleTitle><Pagination><MedlinePgn>6699-703</MedlinePgn></Pagination><Abstract><AbstractText>The complete amino acid sequence of pig liver thioltransferase has been determined. The homogeneous protein was cleaved by trypsin, chymotrypsin, Staphylococcus aureus V8 protease, and cyanogen bromide. The resulting peptides were purified by reversed-phase high performance liquid chromatography and ion-exchange fast protein liquid chromatography. Sequencing of the fragments was achieved with either automated Edman degradation or fast atom bombardment-mass spectrometry. Pig liver thioltransferase is a single polypeptide with 105 amino acid residues and an acetylated glutamine N terminus. The protein has 2 cysteine pairs with sequences of -Cys-Pro-Phe-Cys- and -Cys-Ile-Gly-Gly-Cys-, the first pair of which (Cys22 and Cys25) is located at the potential active site of the enzyme. The sequence of pig liver thioltransferase displays close homology (82%) with calf thymus glutaredoxin, suggesting that they belong to the same evolutionary family.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gan</LastName><ForeName>Z R</ForeName><Initials>ZR</Initials></Author><Author ValidYN="Y"><LastName>Wells</LastName><ForeName>W W</ForeName><Initials>WW</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>AM 32930</GrantID><Acronym>AM</Acronym><Agency>NIADDK NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>RR-00480</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.4</RegistryNumber><NameOfSubstance UI="D014357">Trypsin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008099" MajorTopicYN="N">Liver</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="Y">Protein Disulfide Reductase (Glutathione)</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014357" MajorTopicYN="N">Trypsin</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1987</Year><Month>5</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1987</Year><Month>5</Month><Day>15</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1987</Year><Month>5</Month><Day>15</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">3571278</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Gan, Z R" sort="Gan, Z R" uniqKey="Gan Z" first="Z R" last="Gan">Z R Gan</name><name sortKey="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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