Takahashi M, Banno Y, Nozawa Y
Department of Biochemistry, Gifu University School of Medicine, Japan.
J Med Vet Mycol. 1991;29(3):193-204.
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.
白色念珠菌在培养过程中以不同速率分泌三种类型的磷脂酶（溶血磷脂酶、溶血磷脂酶转酰基酶和磷脂酶B）。白色念珠菌的临床分离株显示出这些磷脂酶的活性各不相同。从白色念珠菌3125的培养滤液中纯化出两种形式的溶血磷脂酶转酰基酶（LPTA）并达到均一性。这两种纯化的酶分别命名为LPTA-I和LPTA-II，它们在分子量（LPTA-I为81 kDa，LPTA-II为41 kDa）、氨基酸组成和酶学性质上存在一些差异。针对纯化的白色念珠菌LPTA-II产生的抗体与LPTA-II反应强烈，但与LPTA-I不反应。此外，白色念珠菌溶血磷脂酶转酰基酶的生化特性与相应的哺乳动物酶不同。
