PHOSPHATE INCORPORATION INTO ALKALINE PHOSPHATASE OF E. COLI
- 1 December 1961
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 47 (12) , 1996-2005
- https://doi.org/10.1073/pnas.47.12.1996
Abstract
Highly purified E. coli alkaline phosphatase reacts with inorganic phosphate yielding serine phosphate and serine -phosphate -containing peptides on partial acid hydrolysis. After digestion of the enzyme with trypsin only one major component contained radio-activity. This product may be degraded by acid hydrolysis to serine phosphate and the same peptides obtained from hydrolysis of the whole enzyme. The phosphate -binding serine most likely is in the active center of the enzymes. Methods of preparation of the enzyme and identification of the products of hydrolysis are given.Keywords
This publication has 15 references indexed in Scilit:
- Genetic control of repression of alkaline phosphatase in E. coliJournal of Molecular Biology, 1961
- An amino acid sequence in the active centre of phosphoglucomutaseBiochemical Journal, 1961
- The Pathway of Carbonate in the Biosynthesis of Carbamyl PhosphateJournal of Biological Chemistry, 1960
- Reversible Phosphate Transfer between Yolk Phosphoprotein and Adenosine TriphosphateJournal of Biological Chemistry, 1960
- A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. Coli I. Purification and characterization of alkaline phosphataseBiochimica et Biophysica Acta, 1960
- The Active Site and Enzyme ActionPublished by Wiley ,1960
- The active site of esterasesJournal of Cellular and Comparative Physiology, 1959
- The grouping of serine phosphate residues in phosvitin and caseinBiochimica et Biophysica Acta, 1959
- Mechanism of Esterase Action: Nature of the Reactive Serine Residue in Enzymes inhibited by Organo-Phosphorus CompoundsNature, 1958
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951