Purification and characterization of lysophospholipase-transacylase (h-LPTA) from a highly virulent strain of Candida albicans.

@article{Mirbod1995PurificationAC,
  title={Purification and characterization of lysophospholipase-transacylase (h-LPTA) from a highly virulent strain of Candida albicans.},
  author={F Mirbod and Y. Banno and Mahmoud Afif Ghannoum and A S Ibrahim and Satoru Nakashima and Yoshimitsu Kitajima and Garry T. Cole and Yoshinori Nozawa},
  journal={Biochimica et biophysica acta},
  year={1995},
  volume={1257 2},
  pages={181-8}
}
A lysophospholipase-transacylase (h-LPTA) was purified to homogeneity from a clinical isolate of Candida albicans (C. albicans) that had high extracellular phospholipase activity (strain 16240). The purified enzyme was a glycoprotein with molecular mass of 84 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The specific activities of the enzyme were 117 mumol/min per mg protein for fatty acid release and 459 mumol/min per mg protein for phosphatidylcholine (PC) formation. An… CONTINUE READING

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