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Alkaline phosphatase ofDrosophila melanogaster. I. Partial purification and characterization

✍ Scribed by Robert A. Harper; F. B. Armstrong


Publisher
Springer
Year
1972
Tongue
English
Weight
488 KB
Volume
6
Category
Article
ISSN
0006-2928

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πŸ“œ SIMILAR VOLUMES


Purification and partial characterizatio
✍ Per Γ…ke Holmgren; Torgny Stigbrand; Gunhild Beckman πŸ“‚ Article πŸ“… 1977 πŸ› Springer 🌐 English βš– 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 Γ…ke Holmgren; Torgny Stigbrand πŸ“‚ Article πŸ“… 1976 πŸ› Springer 🌐 English βš– 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

Rudimentary locus ofDrosophila melanogas
✍ Virginia M. Brothers; Stuart I. Tsubota; Susan E. Germeraad; James W. Fristrom πŸ“‚ Article πŸ“… 1978 πŸ› Springer 🌐 English βš– 619 KB

Glutamine-dependent CPSase, ATCase, and DHOase from Drosophila, the first three enzymes in pyrimidine biosynthesis, show coordinate variation in activity throughout development. The three activities were highest in first instar larvae and decreased as development proceeded. The three activities cose