Catalytic properties and stability of three common variants of placental alkaline phosphatase |
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Authors: | Per Åke Holmgren Torgny Stigbrand |
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Institution: | (1) Department of Physiological Chemistry, University of Umeå, S-901 87 Umeå, Sweden |
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Abstract: | Three placental alkaline phosphatases purified to homogeneity, i.e., the F, I, and S variants, were investigated for catalytic and stability properties. All three forms of the enzyme were found to have almost identical pH optima (10.7–10.8), similar sensitivity to the uncompetitive inhibitors L-phenylalanine (70%) and L-leucine (30%), and identical Km values against p-nitrophenylphosphate, -glycerophosphate, and -naphthylphosphate. Significant differences among the three types were observed in thermal stability. The F variant was found to be most stable and the I variant most labile at 79 C. At 70 C all three forms were stable.This investigation was supported by grants from the Swedish Medical Research Council (Projects No. 4217 and 03X-2725), from the Medical Faculty, University of Umeå, and Jubileumsklinikens i Umeå forskningsfond. |
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Keywords: | placental alkaline phosphatase alkaline phosphatase variants |
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