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. 1977 Jun;15(5-6):521-30.
doi: 10.1007/BF00520195.

Purification and partial characterization of the I variant of placental alkaline phosphatase

P A Holmgren, T Stigbrand, G Beckman

Purification and partial characterization of the I variant of placental alkaline phosphatase

P A Holmgren et al. Biochem Genet. 1977 Jun.

Abstract

The I variant of placental alkaline phosphatase was purified to homogeneity by means of DEAE-cellulose chromatography, isoelectric focusing, and gel filtration on AcA-34. The specific activity of the I variant was found to be 3.33 micronkat/mg. The enzyme is a dimer with an isoelectric point of 4.6 and a molecular weight of 120,000 as determined by sodium dodecylsulfate electrophoresis. The amino acid composition and other physiocochemical properties of the I variant were compared with those of the more common F and S variants. The low activity associated with the I variant is apparently not due to a low specific activity, but to decreased molecular stability. The behavior in the ultracentrifuge and other observations suggest that the I variant differs from the F and S variants in surface charge distribution.

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