
TY  - JOUR
A1  - Murdoch, RN 
A1  - E Buxton, Louise 
A1  - Kay, DJ 
T1  - Mouse Uterine Alkaline Phosphatase: Improved Purification by Affinity Chromatography and Further Characterization of the Enzyme
JF  - Australian Journal of Biological Sciences
JO  - Aust. Jnl. Of Bio. Sci.
Y1  - 1980
VL  - 33
IS  - 3
SP  - 279
EP  - 294
KW  - 
UR  - https://doi.org/10.1071/BI9800279 
N2  - An improved procedure for the purification of alkaline phosphatase from about 10 g of day 7 pregnant mouse uterine tissue is described. Following homogenization, the procedure involved solubilization and extraction with 0·8% (v/v) Triton X-lOO and 20% (v/v) n-butanol, ammonium sulfate precipitation, concanavalin A-Sepharose 4B affinity chromatography, DEAE-cellulose anion-exchange chromatography and Sephacryl S200 gel filtration. On subjecting 2162-fold purified enzyme preparations to polyacrylamide-gel electrophoresis, a single band of protein coincident with the zone of enzyme activity and having an apparent molecular weight of 205 OOO± lOOOO was identified. Affinity chromatography yielded the largest increase in purity of any step in the procedure and established the glycoprotein nature of the uterine enzyme. 
ER  -

