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. 1955 Aug;60(4):573–582. doi: 10.1042/bj0600573

Some properties of alkaline phosphatase of cow's milk and calf intestinal mucosa

R K Morton 1,*
PMCID: PMC1216155  PMID: 13249951

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Selected References

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

  1. AKAMATSU S., ASO Y. Coenzyme of alkaline phosphomonoesterase. Enzymologia. 1953 Dec 30;16(4):231–236. [PubMed] [Google Scholar]
  2. AKAMATSU S., KOBAYASHI K. Chemical nature of the co-phosphomono-esterase. Enzymologia. 1951 Nov;15(3):154–157. [PubMed] [Google Scholar]
  3. CHUNG C. W., NICKERSON W. J. Polysaccharide syntheses in growing yeasts. J Biol Chem. 1954 May;208(1):395–407. [PubMed] [Google Scholar]
  4. Delory G. E. A sodium carbonate-bicarbonate buffer for alkaline phosphatases. Biochem J. 1945;39(3):245–245. [PMC free article] [PubMed] [Google Scholar]
  5. 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]
  6. Dubois K. P., Cochran K. W., Mazur M. Inhibition of Phosphatases by Beryllium and Antagonism of the Inhibition by Manganese. Science. 1949 Oct 21;110(2860):420–422. doi: 10.1126/science.110.2860.420. [DOI] [PubMed] [Google Scholar]
  7. GOMORI G. The complex nature of alkaline phosphatase. Biochim Biophys Acta. 1952 Feb;8(2):162–172. doi: 10.1016/0006-3002(52)90026-7. [DOI] [PubMed] [Google Scholar]
  8. Goodwin T. W., Morton R. A. The spectrophotometric determination of tyrosine and tryptophan in proteins. Biochem J. 1946;40(5-6):628–632. doi: 10.1042/bj0400628. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. HANES C. S., ISHERWOOD F. A. Separation of the phosphoric esters on the filter paper chromatogram. Nature. 1949 Dec 31;164(4183):1107-12, illust. doi: 10.1038/1641107a0. [DOI] [PubMed] [Google Scholar]
  10. Kabat E. A. ASSOCIATION OF PHOSPHATASE WITH A MATERIAL IN KIDNEY SEDIMENTABLE AT HIGH SPEED AND ITS LIBERATION BY AUTOLYSIS. Science. 1941 Jan 10;93(2402):43–44. doi: 10.1126/science.93.2402.43. [DOI] [PubMed] [Google Scholar]
  11. LEHNINGER A. L. Role of metal ions in enzyme systems. Physiol Rev. 1950 Jul;30(3):393–429. doi: 10.1152/physrev.1950.30.3.393. [DOI] [PubMed] [Google Scholar]
  12. LINDENBAUM A., WHITE M. R., SCHUBERT J. Studies on the mechanism of protection by aurintricarboxylic acid in beryllium poisoning. III. Correlation of molecular structure with reversal of biologic effects of beryllium. Arch Biochem Biophys. 1954 Sep;52(1):110–132. doi: 10.1016/0003-9861(54)90093-4. [DOI] [PubMed] [Google Scholar]
  13. LORA-TAMAYO M., ALVAREZ E. F. Coenzyme of kidney phosphatase. Nature. 1954 Mar 20;173(4403):548–549. doi: 10.1038/173548b0. [DOI] [PubMed] [Google Scholar]
  14. MARKHAM R., SMITH J. D. Structure of ribonucleic acid. Nature. 1951 Sep 8;168(4271):406–408. doi: 10.1038/168406a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. MORTON R. K. Alkaline phosphatase of milk. 1. Association of the enzyme with a particulate lipoprotein complex. Biochem J. 1953 Dec;55(5):786–795. doi: 10.1042/bj0550786. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. 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]
  17. 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]
  18. 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]
  19. 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]
  20. 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]
  21. Neuberger A. Carbohydrates in protein: The carbohydrate component of crystalline egg albumin. Biochem J. 1938 Sep;32(9):1435–1451. doi: 10.1042/bj0321435. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. ROCHE J., BOUCHILLOUX S. Sur la purification de la phosphatase alcaline (intestin) et son électrophorèse sur papier. Bull Soc Chim Biol (Paris) 1953;35(7):567–573. [PubMed] [Google Scholar]
  23. ROCHE J., BOUCHILLOUX S. Sur la purification de la phosphatase alcaline (intestin). Bull Soc Chim Biol (Paris) 1950;32(9-10):732–738. [PubMed] [Google Scholar]
  24. SANADI D. R. Enzymatic dephosphorylation of triphosphopyridine nucleotide. Arch Biochem Biophys. 1952 Feb;35(2):268–277. doi: 10.1016/s0003-9861(52)80006-2. [DOI] [PubMed] [Google Scholar]
  25. SCHUBERT J., LINDENBAUM A. Studies on the mechanism of protection by aurintricarboxylic acid in beryllium poisoning. II. Equilibria involving alkaline phosphatase. J Biol Chem. 1954 May;208(1):359–368. [PubMed] [Google Scholar]
  26. TAMAYO M. L., MUNICIO A. M. Coenzyme of kidney phosphatase. Nature. 1951 Aug 11;168(4267):249–249. doi: 10.1038/168249a0. [DOI] [PubMed] [Google Scholar]
  27. VEERKAMP T. A., SMITS G. Mode of action of beryllium on alkaline phosphatase. Nature. 1953 Sep 26;172(4378):589–590. doi: 10.1038/172589a0. [DOI] [PubMed] [Google Scholar]
  28. 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]

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