| The amino acid sequence of cytosolic aspartate aminotransferase from human liver. | |
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MedLine Citation:
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PMID: 2241899 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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1. The cytosolic aspartate aminotransferase was purified from human liver. 2. The isoenzyme contains four cysteine residues, only one of which reacts with 5,5'-dithiobis-(2-nitrobenzoic acid) in the absence of denaturing agents. 3. The amino acid sequence of the isoenzyme is reported, as determined from peptides produced by digestion with trypsin and with CNBr, and from sub-digestion of some of these peptides with Staphylococcus aureus V8 proteinase. 4. The isoenzyme shares 48% identity of amino acid sequence with the mitochondrial form from human heart. 5. Comparisons of the amino acid sequences of all known mammalian cytosolic aspartate aminotransferases and of the same set of mitochondrial isoenzymes are reported. The results indicate that the cytosolic isoenzymes have evolved at about 1.3 times the rate of the mitochondrial forms. 6. The time elapsed since the cytosolic and mitochondrial isoenzymes diverged from a common ancestral protein is estimated to be 860 x 10(6) years. 7. Experimental details and confirmatory data for the results presented here are given in a supplementary paper that has been deposited as a Supplementary Publication SUP 50158 (25 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1990) 265, 5. |
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Authors:
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J M Doyle; M E Schininà; F Bossa; S Doonan |
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Publication Detail:
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Type: Comparative Study; Journal Article |
Journal Detail:
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Title: The Biochemical journal Volume: 270 ISSN: 0264-6021 ISO Abbreviation: Biochem. J. Publication Date: 1990 Sep |
Date Detail:
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Created Date: 1990-12-06 Completed Date: 1990-12-06 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 651-7 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, University College, Cork, Ireland. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Aspartate Aminotransferases / chemistry*, isolation & purification Cyanogen Bromide / chemistry Cysteine / analysis Cytosol / enzymology Humans Liver / enzymology* Metalloendopeptidases / metabolism Mitochondria / enzymology Molecular Sequence Data Peptide Mapping Trypsin |
| Chemical | |
Reg. No./Substance:
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506-68-3/Cyanogen Bromide; 52-90-4/Cysteine; EC 2.6.1.1/Aspartate Aminotransferases; EC 3.4.21.4/Trypsin; EC 3.4.24.-/Metalloendopeptidases; EC 3.4.24.29/auR protein, Staphylococcus aureus |
| Comments/Corrections | |
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