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Partial purification and some characteristics of hamster molar alkaline phosphatase

✍ Scribed by A. A. Dogterom; D. M. Lyaruu; A. Doderer; J. H. M. Wöltgens


Publisher
Springer
Year
1984
Tongue
English
Weight
487 KB
Volume
40
Category
Article
ISSN
1420-682X

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📜 SIMILAR VOLUMES


Purification and partial characterizatio
✍ Per Åke Holmgren; Torgny Stigbrand; Gunhild Beckman 📂 Article 📅 1977 🏛 Springer 🌐 English ⚖ 461 KB

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

Purification and partial characterizatio
✍ 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

Partial purification and some properties
✍ H. Khyami-Horani 📂 Article 📅 1996 🏛 Springer 🌐 English ⚖ 532 KB

A newly isolated Bacillus species, which grew optimally at 30°C and pH 10, produced a carboxymethylcellulase in a medium containing 10 g CM-cellulose/l. The enzyme, when partially purified by gel filtration, had a mass of about 29 kDa as determined by both SDS-PAGE and gel filtration chromatography.