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. 1955 Oct;61(2):232–240. doi: 10.1042/bj0610232

The substrate specificity and inhibition of alkaline phosphatases of cow's milk and calf intestinal mucosa

R K Morton 1,*
PMCID: PMC1215777  PMID: 13260203

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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 determination of enzyme inhibitor constants. Biochem J. 1953 Aug;55(1):170–171. doi: 10.1042/bj0550170. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. 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]
  3. 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]
  4. Eggleton P., Elsden S. R., Gough N. The estimation of creatine and of diacetyl. Biochem J. 1943;37(5):526–529. doi: 10.1042/bj0370526. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ennor A. H., Stocken L. A. The preparation of sodium phosphocreatine. Biochem J. 1948;43(2):190–191. [PMC free article] [PubMed] [Google Scholar]
  6. HOLTER H., LIS S. O. Determination and properties of phosphoamidase. C R Trav Lab Carlsberg Chim. 1951;27(16-17):393–407. [PubMed] [Google Scholar]
  7. 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]
  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 action of purified alkaline phosphatases on di- and tri- phosphopyridine nucleotides. Biochem J. 1955 Oct;61(2):240–244. doi: 10.1042/bj0610240. [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. Transferase activity of hydrolytic enzymes. Nature. 1953 Jul 11;172(4367):65–68. doi: 10.1038/172065a0. [DOI] [PubMed] [Google Scholar]
  13. Mackworth J. F., Webb E. C. The inhibition of serum cholinesterase by alkyl fluorophosphonates. Biochem J. 1948;42(1):91–95. doi: 10.1042/bj0420091. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Needham D. M. The adenosinetriphosphatase activity of myosin preparations. Biochem J. 1942 Feb;36(1-2):113–120. doi: 10.1042/bj0360113. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. WALSH E. O. Thiophosphates as possible intermediates in phosphate transfer. Nature. 1952 Mar 29;169(4300):546–546. doi: 10.1038/169546a0. [DOI] [PubMed] [Google Scholar]
  16. WEIL-MALHERBE H., GREEN R. H. The catalytic effect of molybdate on the hydrolysis of organic phosphate bonds. Biochem J. 1951 Aug;49(3):286–292. [PMC free article] [PubMed] [Google Scholar]
  17. Webb E. C. The action of alkyl fluorophosphonates on esterases and other enzymes. Biochem J. 1948;42(1):96–98. doi: 10.1042/bj0420096. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. ZITTLE C. A., DELLAMONICA E. S. Use of butanol in the purification of the alkaline phosphatase of bovine milk. Arch Biochem Biophys. 1952 Feb;35(2):321–325. doi: 10.1016/s0003-9861(52)80011-6. [DOI] [PubMed] [Google Scholar]

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