FIDELIO GERARDO DANIEL
Artículos
Título:
Kinetic characterization, optimum conditions for catalysis and substrate preference of secretory phospholipase A 2 from Glycine max in model membrane systems
Autor/es:
MARIANI, M.E.,; MADOERY, R.; FIDELIO, GD.
Editorial:
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
Referencias:
Lugar: Paris; Año: 2015 vol. 108 p. 48 - 48
Resumen:
b s t r a c tTwo secretory phospholipase A 2 (sPLA 2 s) from Glycine max, GmsPLA 2 -IXA-1 and GmsPLA 2 -XIB-2, have been purified as recombinant proteins and the activity was evaluated in order to obtain the optimum conditions for catalysis using mixed micelles and lipid monolayers as substrate. Both sPLA 2 s showed a maximum enzyme activity at pH 7 and a requirement of Ca 2þ in the micromolar range. These parameters were similar to those found for animal sPLA 2 s but a surprising optimum temperature for catalysis at 60 °C was observed. The effect of negative interfacial charges on the hydrolysis of organized substrates was evaluated through initial rate measurements using short chain phospholipids with different head groups. The enzymes showed subtle differences in the specificity for phospholipids with different head groups (DLPC, DLPG, DLPE, DLPA) in presence or absence of NaCl. Both recombinant enzymes showed lower activity toward anionic phospholipids and a preference for