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Biochemical characterization and inhibitory effects of dinophysistoxin-1, okadaic acid and microcystine l-r on protein phosphatase 2a purified from the mussel Mytilus chilensis. Biol. Res.
RIVAS,MARIELLA; GARCÍA,CARLOS; LIBERONA,JOSÉ L; LAGOS,NÉSTOR.
Protein phosphatases are involved in many cellular processes. One of the most abundant and best studied members of this class is protein phosphatase type-2A (PP2A). In this study, PP2A was purified from the mussel Mytilus chilensis. Using both SDS-PAGE and size exclusion gel filtration under denaturant conditions, it was confirmed that the PP2A fraction was essentially pure. The isolated enzyme is a heterodimer and the molecular estimated masses of the subunits are 62 and 28 kDa. The isolated PP2A fraction has a notably high p-NPP phosphatase activity, which is inhibited by NaCl. The hydrolytic p-NPP phosphatase activity is independent of the MgCl2 concentration. The time courses of the inhibition of the PP2A activity of p-NPP hydrolysis by increasing...
Tipo: Journal article Palavras-chave: Chile; Diarrhetic Shellfish Poisoning (DSP); Mussel; Mytilus chilensis; Protein Phosphatase 2A; Microcystine L-R.
Ano: 2000 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602000000300005
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