Partial Purification of Bovine Intestinal Alkaline Phosphatase.
- 1 December 1952
- journal article
- research article
- Published by Frontiers Media SA in Experimental Biology and Medicine
- Vol. 81 (3), 593-596
- https://doi.org/10.3181/00379727-81-19952
Abstract
The microsome fraction of homogenates of intestinal mucosa was isolated by differential centrifugation. In confirmation of previous reports, this fraction contains almost all of the alkaline phosphatase, with a specific activity between 3 and 5 times that of the original homogenate. A soluble prepn. may be obtained by treating a microsome suspension with n-butanol, according to the method of R. K. Morton. The behavior of the soluble prepn. on acetone precipitation is reported, as well as filter paper electrophoresis results with the same prepn. Both types of examination indicate that less than 10% of the soluble prepn. can be phosphatase, but it appears to be particularly suitable for further fractionation.Keywords
This publication has 4 references indexed in Scilit:
- Use of butanol in the purification of the alkaline phosphatase of bovine milkArchives of Biochemistry and Biophysics, 1952
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- Substrate specificities and inhibition of intra cellular alkaline phosphatases associated with cytoplasmic granules sedimented by differential centrifugationJournal of Cellular and Comparative Physiology, 1951
- Über die Nierenphosphatase. (1. Mitteilung zur Kenntnis der Phosphatasen.)Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1935