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"MEDLINE" . "1985-10-09" . "1985-10-09" . "2007-12-19" . "97" . "97" . "1985 May" . "1985-05" . "Aspartate aminotransferase isozymes from rabbit liver. Purification and properties." . "Aspartate aminotransferase isozymes from rabbit liver. Purification and properties." . "1337-45" . "1337" . "Cytosolic and mitochondrial isozymes of aspartate aminotransferase (L-aspartate:2-oxoglutarate aminotransferase [EC 2.6.1.1] ) were purified to homogeneity from rabbit liver. The rabbit liver isozymes were closely similar to the corresponding isozymes from other sources, including human heart, pig heart, chicken heart, and rat liver, in their molecular weights, absorption spectra, amino acid compositions, isoelectric points, and Michaelis constants for the substrates. The NH2-terminal amino acid sequences of rabbit liver isozymes were identified up to 30 residues, and showed some differences from those of the corresponding isozymes obtained from other animals so far studied." . "" . 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Purification and properties. http://purl.uniprot.org/core/volume 97 http://www.w3.org/1999/02/22-rdf-syntax-ns#type http://bio2rdf.org/core:Journal_Citation http://www.w3.org/2002/07/owl#sameAs http://bio2rdf.org/medline:85289123 http://bio2rdf.org/pubmed:4030726 }}} ==== Pubmed Linked Data @Uniprot ==== http://www.uniprot.org/citations/4030726.rdf {{{ @prefix @prefix rdf @prefix rdfs @prefix owl @prefix skos @prefix pubmed pubmed:4030726 rdf:type Journal_Citation title "Aspartate aminotransferase isozymes from rabbit liver. Purification and properties." author "Kuramitsu S." author "Inoue K." author "Kondo K." author "Aki K." author "Kagamiyama H." skos:exactMatch skos:exactMatch pubmed:4030726 date 1985 rdfs:comment "Cytosolic and mitochondrial isozymes of aspartate aminotransferase (L-aspartate:2-oxoglutarate aminotransferase [EC 2.6.1.1] ) were purified to homogeneity from rabbit liver. The rabbit liver isozymes were closely similar to the corresponding isozymes from other sources, including human heart, pig heart, chicken heart, and rat liver, in their molecular weights, absorption spectra, amino acid compositions, isoelectric points, and Michaelis constants for the substrates. The NH2-terminal amino acid sequences of rabbit liver isozymes were identified up to 30 residues, and showed some differences from those of the corresponding isozymes obtained from other animals so far studied." name "J. Biochem." volume 97 pages "1337-1345" }}}