Abstract
The phosphate-repressible acid phosphatase from Yarrowia lipolytica cells was more thermostable but more sensitive to urea denaturation and to the effect of Triton X-100 than the constitutive counterpart. The K m values of the repressible and constitutive enzymes for p-nitrophenyl phosphate were 3.6 mM and 7.4 mM, respectively. They are judged to be distinct proteins.
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