Selective determination of fish aspartate aminotransferase isoenzymes by their differential sensitivity to proteases (CROSBI ID 85788)
Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija
Podaci o odgovornosti
Petrović, Siniša ; Semenčić, Lorena ; Ozretić, Bartolo ; Krajnović-Ozretić, Mirjana
engleski
Selective determination of fish aspartate aminotransferase isoenzymes by their differential sensitivity to proteases
Various proteases (proteinase K, subtilisin, trypsin and chymotrypsin) were used to study the selective inactivation of the aspartate aminotransferase (EC 2.6.1.1) isoenzymes of grey mullet (Mugil auratus Risso ; Osteichthyes). The cytosolic isoenzyme was significantly inactivated by proteinase K, subtilisin and chymotrypsin, while the mitochondrial isoenzyme was sensitive only to proteinase K and to high doses of trypsin. Further identification of the aspartate aminotransferase isoenzymes was based on their discrete sensitivity toward chymotrypsin. Chymotrypsin (1 mg/ml) successfully inhibited purified cytosolic aspartate aminotransferase as well as cytosolic isoenzyme from plasma, whereas the mitochondrial form persisted unaffected. Similar results were obtained when examining liver and red muscle homogenates. This method revealed that the increased total activity of aspartate aminotransferase in fish plasma with induced acute liver injury, was partially a result of the mitochondrial isoenzyme leakage from damaged tissue
aspartate aminotransferase(AAT) ; chymotrypsin ; cytosolic AAT ; enzyme inactivation ; fish plasma
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Podaci o izdanju
124 (1)
1999.
209-214
objavljeno
1096-4959
1879-1107
10.1016/S0305-0491(99)00119-4