Pregled bibliografske jedinice broj: 9279
Cytosolic Aspartate Aminotransferase from Grey Mullet (Mugil auratus Risso ) Red Muscle : Isolation and Properties
Cytosolic Aspartate Aminotransferase from Grey Mullet (Mugil auratus Risso ) Red Muscle : Isolation and Properties // International journal of biochemistry & cell biology, 28 (1996), 8; 873-881 doi:10.1016/1357-2725(96)00033-7 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 9279 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Cytosolic Aspartate Aminotransferase from Grey
Mullet (Mugil auratus Risso ) Red Muscle :
Isolation and Properties
(Cytosolic Aspartate Aminotransferase from Grey Mullet
(Mugil auratus Risso ) Red Muscle : Isolation and
Properties)
Autori
Petrović, Siniša ; Ozretić, Bartolo ; Krajnović- Ozretić, Mirjana
Izvornik
International journal of biochemistry & cell biology (1357-2725) 28
(1996), 8;
873-881
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
aspartate aminotransferase ; cytosol ; enzyme purification ; enzyme characterization ; grey mullet
Sažetak
Aspartate aminotransferase isoenzymes play a central role in the metabolism of amino acids and participate in maintaining redox balance via an aspartate-malate shutle in aerobic tissues such as red muscle. The aim of this study was to purify and characterize cytosolic isoenzyme of aspartate aminotransferase from the red muscle of grey mullet , Mugil auratus Risso. The properties of the fish enzyme and its possible physiological role are discussed and compared with homotopic isoenzymes from other species. The enzyme was purified to homogeneity by using different column chromatography techniques and further characterized with gel electrophoresis. It was found to be composed of two identical subunits, M t = 41.000 ą 882 (SEM, n=3). Electrophoretic analysis revealed several active subforms of isolated cytosolic isoenzyme with pI in the pH range 5.2-5.6 .The isolated enzyme was stable in the pH range 5.0- 10.0 and between 0 and 300C. It showed optimum activity at pH 7.5-9.0. Km values of substrates L- aspartate and -ketoglutarate were 1.01 ą 0.082 and 0.031 ą 0.0035 mM, respectively. In the reverse reaction Km values of substrates L- glutamate and oxaloacetate were estimated to be 4.65ą0.90 and 1.22ą0.41mM, respectively. The isolated enzyme was responsible for the transamination of taurine intermediate, L- cysteine sulfinate, in the cytosol of red muscle with apparent Km of 3.08ą0.35 mM. This study demonstrated that cytosolic aspartate aminotransferase isoenzyme from gery mullet red muscle resembles vertebrate cytosolic isoenzymes in its general physicochemical and catalytic properties.
Izvorni jezik
Engleski
Znanstvena područja
Biologija
Citiraj ovu publikaciju:
Časopis indeksira:
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus
- MEDLINE
Uključenost u ostale bibliografske baze podataka::
- PubMed
- Index medicus