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

✍ Scribed by Per Åke Holmgren; Torgny Stigbrand; Gunhild Beckman

Publisher
Springer
Year
1977
Tongue
English
Weight
461 KB
Volume
15
Category
Article
ISSN
0006-2928

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✦ Synopsis

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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Purification and partial characterizatio
Purification and partial characterization of two genetic variants of placental alkaline phosphatase
✍ Per Åke Holmgren; Torgny Stigbrand 📂 Article 📅 1976 🏛 Springer 🌐 English ⚖ 630 KB

The two most common variants of placental alkaline phosphatase, the F and S variants, were purified to homogeneity and characterized. Their molecular weights were determined by equilibrium ultracentrifugation and sodium dodecylsufate polyacrylamide gel electrophoresis, which gave almost identical va

Catalytic properties and stability of th
Catalytic properties and stability of three common variants of placental alkaline phosphatase
✍ Per Åke Holmgren; Torgny Stigbrand 📂 Article 📅 1978 🏛 Springer 🌐 English ⚖ 430 KB

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-phe