Interfacial kinetic and binding properties of the complete set of human and mouse groups I, II, V, X, and XII secreted phospholipases A2.

@article{Singer2002InterfacialKA,
  title={Interfacial kinetic and binding properties of the complete set of human and mouse groups I, II, V, X, and XII secreted phospholipases A2.},
  author={Alan G. Singer and Farideh Ghomashchi and Catherine Le Calvez and James Gerard Bollinger and Sofiane Bezzine and Morgane Rouault and Martin Sad{\'i}lek and E. M. Nguyen and Michel Lazdunski and G{\'e}rard Lambeau and Michael H Gelb},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 50},
  pages={
          48535-49
        }
}
Expression of the full set of human and mouse groups I, II, V, X, and XII secreted phospholipases A(2) (sPLA(2)s) in Escherichia coli and insect cells has provided pure recombinant enzymes for detailed comparative interfacial kinetic and binding studies. The set of mammalian sPLA(2)s display dramatically different sensitivity to dithiothreitol. The specific activity for the hydrolysis of vesicles of differing phospholipid composition by these enzymes varies by up to 4 orders of magnitude, and… CONTINUE READING

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