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. 1957 Apr;65(4):674–682. doi: 10.1042/bj0650674

The kinetics of hydrolysis of phenyl phosphate by alkaline phosphatases

R K Morton 1
PMCID: PMC1199935  PMID: 13426083

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. DIXON M. The effect of pH on the affinities of enzymes for substrates and inhibitors. Biochem J. 1953 Aug;55(1):161–170. doi: 10.1042/bj0550161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Delory G. E., King E. J. The rate of enzymic hydrolysis of phosphoric esters: 2. Relation of structure to dissociation constant, Michaelis constant, and rate of hydrolysis. Biochem J. 1943;37(5):547–550. doi: 10.1042/bj0370547. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Folley S. J., Kay H. D. The alkaline phosphomonoesterase of the mammary gland. Biochem J. 1935 Aug;29(8):1837–1850. doi: 10.1042/bj0291837. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. HOFSTEE B. H. J. On the evaluation of the constants Vm and KM in enzyme reactions. Science. 1952 Sep 26;116(3013):329–331. doi: 10.1126/science.116.3013.329. [DOI] [PubMed] [Google Scholar]
  5. HORWITT B. N. Determination of inorganic serum phosphate by means of stannous chloride. J Biol Chem. 1952 Dec;199(2):537–541. [PubMed] [Google Scholar]
  6. MORTON R. K. Alkaline phosphatase of milk. 2. Purification of the enzyme. Biochem J. 1953 Dec;55(5):795–800. doi: 10.1042/bj0550795. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. MORTON R. K. Microsomal particles of normal cow's milk. Nature. 1953 Apr 25;171(4356):734–735. doi: 10.1038/171734a0. [DOI] [PubMed] [Google Scholar]
  8. MORTON R. K. Separation and purification of enzymes associated with insoluble particles. Nature. 1950 Dec 30;166(4235):1092–1095. doi: 10.1038/1661092a0. [DOI] [PubMed] [Google Scholar]
  9. MORTON R. K. Some properties of alkaline phosphatase of cow's milk and calf intestinal mucosa. Biochem J. 1955 Aug;60(4):573–582. doi: 10.1042/bj0600573. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. MORTON R. K. The lipoprotein particles in cow's milk. Biochem J. 1954 Jun;57(2):231–237. doi: 10.1042/bj0570231. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. MORTON R. K. The purification of aklaline phosphatases of animal tissues. Biochem J. 1954 Aug;57(4):595–603. doi: 10.1042/bj0570595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. MORTON R. K. The substrate specificity and inhibition of alkaline phosphatases of cow's milk and calf intestinal mucosa. Biochem J. 1955 Oct;61(2):232–240. doi: 10.1042/bj0610232. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. MORTON R. K. Transferase activity of hydrolytic enzymes. Nature. 1953 Jul 11;172(4367):65–68. doi: 10.1038/172065a0. [DOI] [PubMed] [Google Scholar]
  14. ROCHE J., SARLES H. Spécificité d'organe des phosphatases alcalines et hyperphosphatasémies. II. Bull Soc Chim Biol (Paris) 1954;36(4-5):491–499. [PubMed] [Google Scholar]
  15. ROSS M. H., ELY J. O., ARCHER J. G. Alkaline phosphatase activity and pH optima. J Biol Chem. 1951 Oct;192(2):561–568. [PubMed] [Google Scholar]

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