Characterization and activity determination of the human protein phosphatase 2A catalytic subunit α expressed in insect larvae

Applied Biochemistry and Biotechnology

Volumn 167, Issue 4, 2012, Pages 918-928

  Rubiolo, J A ^a,b   Lopez Alonso H ^b   Alfonso, A ^b   Vega, F V ^a   Vieytes, M R ^a   Botana, L M ^b  

^a Departamento de Fisiología   (Spain)

^b Farmacología   (Spain)

Author keywords

Enzyme stability; Okadaic acid; Protein phosphatase 2A inhibition; Recombinant protein phosphatase 2A; Trichoplusia ni

Indexed keywords

ACTIVE PROTEINS; ANIMAL CELLS; ANIMAL TISSUE; BACULOVIRUS; CATALYTIC SUBUNITS; CODING SEQUENCES; DEPHOSPHORYLATES; ENZYME STABILITY; FOSTRIECIN; HUMAN PROTEINS; INSECT LARVAE; NODULARIN; OKADAIC ACID; P-NITROPHENYL PHOSPHATE; POLYHEDRIN; PROTEIN PHOSPHATASE 2A; PROTEIN PURIFICATION; PROTEIN PURITY; PURIFIED PROTEIN; RECOMBINANT EXPRESSION; THREONINE RESIDUES; TRICHOPLUSIA NI; WESTERN BLOTS;

AFFINITY CHROMATOGRAPHY; AMINO ACIDS; CYTOLOGY; ENZYME ACTIVITY; METABOLITES; PURIFICATION; RECOMBINANT PROTEINS; TISSUE; TOXIC MATERIALS;

ENZYME INHIBITION;

4 NITROPHENYL PHOSPHATE; ANTIBIOTIC AGENT; CALYCULIN A; CANTHARIDIN; DINOPHYSISTOXIN 1; FOSTRIECIN; MICROCYSTIN LR; NODULARIN; OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE 2A; POLYHEDRIN; TAUTOMYCIB; UNCLASSIFIED DRUG;

AFFINITY CHROMATOGRAPHY; ANALYTIC METHOD; ANIMAL CELL; ARTHROPOD LARVA; ARTICLE; CONTROLLED STUDY; COST EFFECTIVENESS ANALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME ASSAY; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME SUBUNIT; ENZYME SYNTHESIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN DEPHOSPHORYLATION; PROTEIN EXPRESSION; REPRODUCIBILITY; TOXIN ANALYSIS; TRICHOPLUSIA; WESTERN BLOTTING;

ANIMALS; ENZYME ASSAYS; ENZYME INHIBITORS; GENE EXPRESSION; HUMANS; ISOENZYMES; LARVA; MOTHS; PROTEIN PHOSPHATASE 2; PROTEIN SUBUNITS;

ANIMALIA; DINOPHYSIS; HEXAPODA; PLUSIA; TRICHOPLUSIA NI;

EID: 84863709938     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-012-9737-1     Document Type: Article

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