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  • Title: Secreted Candida albicans phospholipases: purification and characterization of two forms of lysophospholipase-transacylase.
    Author: Takahashi M, Banno Y, Nozawa Y.
    Journal: J Med Vet Mycol; 1991; 29(3):193-204. PubMed ID: 1890563.
    Abstract:
    Candida albicans secreted three types of phospholipase (lysophospholipase, lysophospholipase-transacylase and phospholipase B) at different rates in culture. Clinical isolates of C. albicans showed variable activities of these phospholipases. Two forms of lysophospholipase-transacylase (LPTA) were purified to homogeneity from the culture filtrate of C. albicans 3125. The two purified enzymes, designated LPTA-I and LPTA-II, showed some differences in molecular mass (81 kDa for LPTA-I and 41 kDa for LPTA-II), amino acid composition and enzymatic properties. Antibody raised against purified C. albicans LPTA-II reacted strongly with LPTA-II, but not with LPTA-I. Furthermore, the biochemical properties of C. albicans lysophospholipase-transacylase were distinct from those of the corresponding mammalian enzyme.
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