Abstract
1. Inhibition of the pyrophosphatase and orthophosphatase activities of human liver and small-intestinal alkaline-phosphatase preparations by different classes of inhibitors has been studied. 2. Each type of substrate, pyrophosphate or orthophosphate, is a competitive inhibitor of hydrolysis of the other type. 3. l-Phenylalanine is a non-competitive inhibitor of both types of activity of the intestinal preparation, but inhibits neither activity of the liver enzyme. Arsenate is a competitive inhibitor of both activities of both preparations. For a given inhibitor, the values of Ki are independent of the type of substrate used when measurements are made at the same pH. 4. Mg2+ ions activate orthophosphatase but inhibit pyrophosphatase, except in very low concentrations. 5. These results are compatible with the presence in each tissue preparation of a single enzyme with one type of active centre, possessing both orthophosphatase and pyrophosphatase activities.
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- BLOCH-FRANKENTHAL L. The role of magnesium in the hydrolysis of sodium pyrophosphate by inorganic pyrophosphatase. Biochem J. 1954 May;57(1):87–92. doi: 10.1042/bj0570087. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DELSAL J. L., MANHOURI H. Etude comparative des dosages colorimétriques du phosphore. IV. Dosage de l'orthophosphate en présence d'esters phosphoriques; nouvelles méthodes. Bull Soc Chim Biol (Paris) 1958;40(11):1623–1636. [PubMed] [Google Scholar]
- 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]
- Delory G. E. A sodium carbonate-bicarbonate buffer for alkaline phosphatases. Biochem J. 1945;39(3):245–245. [PMC free article] [PubMed] [Google Scholar]
- FISHMAN W. H., GREEN S., INGLIS N. I. Organ-specific behavior exhibited by rat intestine and liver alkaline phosphatase. Biochim Biophys Acta. 1962 Aug 13;62:363–375. doi: 10.1016/0006-3002(62)90266-4. [DOI] [PubMed] [Google Scholar]
- MOSS D. W., CAMPBELL D. M., ANAGNOSTOU-KAKARAS E., KING E. J. Characterization of tissue alkaline phosphatases and their partial purification by starch-gel electrophoresis. Biochem J. 1961 Nov;81:441–447. doi: 10.1042/bj0810441. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MOTZOK I. Studies on alkaline phosphatases. I. Kinetics of plasma phosphatase of normal and rachitic chicks. Biochem J. 1959 May;72(1):169–177. doi: 10.1042/bj0720169. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Moss D. W. A note on the spectrophotometric estimation of alkaline phosphatase activity. Enzymologia. 1966 Oct 31;31(4):193–202. [PubMed] [Google Scholar]
- Moss D. W., Eaton R. H., Smith J. K., Whitby L. G. Association of inorganic-pyrophosphatase activity with human alkaline-phosphatase preparations. Biochem J. 1967 Jan;102(1):53–57. doi: 10.1042/bj1020053. [DOI] [PMC free article] [PubMed] [Google Scholar]