A comparison of the alkaline phosphatases of rat dental pulp, bone, kidney, liver and intestine.
The sensitivity of the dental pulp enzyme to heat was similar to that of enzymes from bone and kidney; alkaline phosphatases from liver and intestine were more stable to heat. L-Homoarginine strongly inhibited the enzyme activities from pulp, bone, kidney and liver but did not affect intestinal enzyme activity. Increasing the molarity of carbonate buffer or glycine buffer in the assay solution decreased intestinal alkaline phosphatase activity more markedly than enzyme activities of other tissues. In 100 mM glycine-NaOH buffer, the effects of Zn2+, Mg2+ and Ca2+ on pulp alkaline phosphatase activity were similar to those on the enzyme activities of bone, kidney and liver. The electrophoretic pattern of the pulp enzyme on sodium dodecyl sulphate-gels was identical with that of bone enzyme and differed from the patterns of enzymes from other tissues. These results suggest that the dental pulp alkaline phosphatase may be the same as bone enzyme.
D000469:Alkaline Phosphatase / Q000378:metabolism*; D000818:Animals; D001842:Bone and Bones / Q000201:enzymology; D002413:Cations, Divalent / Q000494:pharmacology; D003782:Dental Pulp / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D006709:Homoarginine; D007413:Intestinal Mucosa / Q000201:enzymology; D007672:Kidney Cortex / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D008297:Male; D009994:Osmolar Concentration; D051381:Rats; D011919:Rats, Inbred Strains
D002413:Cations, Divalent; D006709:Homoarginine; D000469:Alkaline Phosphatase