PMID: 9454Sep 1, 1976

A comparison of ATP-degrading enzyme activities in rat incisor odontoblasts

The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society
G Granström, A Linde


In active odontoblasts from the rat incisor, used as a model system for biologic calcification, two distinguishable enzyme activities capable of degrading adenosine monophosphate (ATP) exist. Once can be inhibited ny 1-tetramisole, (+/-)-2,3,5,6,-tetrahydro-6-phenylimidazo (2.1B) THIAZOLE HYDROCHLORIDE (Levamisol) and (+/-)-6(m-bromophenyl)-5.6-dehydroimidazo (2.1-b) thiazole oxalate (R823) and is probably identical with nonspecific alkaline phosphatase (EC The activity of the other enzyme, named Ca2+-ATPase, is dependent on the presence of Ca2+ or Mg2+ and is activated by these ions. The pH optimum of Ca2+-ATPase is 9.8. The Ca2+-ATPase is unaffected by Levamisole, R 8231, ouabain, ruthenium red, Na+ and K+ ions. Maximal activity was found against ATP, whereas adenosine diphosphate, guanosine triphosphate, inosine triphosphate and adensoine monophosphate were hydrolysed at lower rate. It may be speculated that the Ca2+-ATPase is concerned with the transmembranous transport of Ca2+ ions to the mineralization front.


Jan 1, 1981·Calcified Tissue International·G Granström, A Linde
Nov 1, 1977·Journal of Oral Pathology·C EngströmB C Magnusson
Feb 1, 1980·Experimental Neurology·E Marani
Jan 1, 1979·Archives of Oral Biology·I Läikkö, M Larmas
Jan 1, 1979·Archives of Oral Biology·R Nilsen, B C Magnusson
Jun 1, 1982·Acta Orthopaedica Scandinavica·C Engström, G Granström
Feb 1, 1981·Journal of Dental Research·Y Le Bell
Jan 1, 1982·Acta Odontologica Scandinavica·G Granström
Jan 1, 1978·Scandinavian Journal of Dental Research·H Mörnstad
Jan 1, 1993·Critical Reviews in Oral Biology and Medicine : an Official Publication of the American Association of Oral Biologists·A Linde, M Goldberg

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Alkaline Phosphatase
Enzyme Activation
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