Secreted Candida albicans phospholipases: purification and characterization of two forms of lysophospholipase-transacylase.
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.
Takahashi
M
M
Department of Biochemistry, Gifu University School of Medicine, Japan.
Banno
Y
Y
Nozawa
Y
Y
D000217:Acyltransferases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D002176:Candida albicans / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D006863:Hydrogen-Ion Concentration; D007124:Immunoenzyme Techniques; D008245:Lysophospholipase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D010713:Phosphatidylcholines / Q000276:immunology / Q000378:metabolism
D000596:Amino Acids; D009097:Multienzyme Complexes; D010713:Phosphatidylcholines; D000217:Acyltransferases; D008245:Lysophospholipase; C021782:lysophospholipase-transacylase