Purification and isolation of 2 phosphatases from sheep liver

F. Ponz
J. Prous
131

Abstract




The levels of purífication of phosphatases (ortophosphoric monoester phosphydrolases, 3.1.3.1, 3.1.3.2) from the liver were much below those obtained from other sources. A method is described which ineludes as a fundamental step the treat- ment with ion-exchange adsorbents (like to Dowex 50 and Dowex 3), a great quantity of inert protein being retained in the anionic resin. The resulting solution is precipitated by (NJD2SO4 between 45-85 % saturation, redisolved and then precipitated with acetone (60 %). Dissolved in water it is cro- matografied on paper (ethanol-water, 1 : 1), where two frac- tions are distinguished (Rr 0.48 and 0.37) with optimal pH 9.8 and 6 respectively, which can be recovered by elution





Preparations of alkaline phosphatase are by this way obtained with optimal 9.8, specific activity 28.000 units (/xg P/mg N/min) and of acid phosphatase with optimal 6, specific activity 33.000 units. The purification is with respect to theinitial homogenate of some 600 and 1.000 times respectively.





 




Keywords:
LIVER, Liver, PHOSPHATASES, Phosphoric Monoester Hydrolases, SHEEP, Sheep, Animals, Domestic

Authors

F. Ponz
J. Prous


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