Similarities between alkaline phosphatase and Ca2+ ATPase activities in HeLa cells.
Parallel changes in the enzyme activities of CA2+ATPase and alkaline phosphatase were observed in HeLa cells. Both enzymes were inhibited to a similar degree by L-phenylalanine, L-tryptophan, and L-leucine, while being relatively resistant to L-homoarginine. Exposure to heat (56 degrees C, 60 degrees C, and 65 degrees C) resulted in a loss of both enzyme activities. Both alkaline phosphatase and Ca2+ ATPase, when treated with EGTA, required Ca2+ for the restoration of activity. Cells grown in the presence of agents that affect alkaline phosphatase (dexamethasone, butyric acid, and hyperosmolar NaCl) showed similar changes in the activities of both enzymes.
D000469:Alkaline Phosphatase / Q000302:isolation & purification / Q000378:metabolism*; D000596:Amino Acids / Q000494:pharmacology; D002118:Calcium / Q000494:pharmacology; D000252:Calcium-Transporting ATPases / Q000302:isolation & purification / Q000378:metabolism*; D006367:HeLa Cells; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D013347:Subcellular Fractions / Q000201:enzymology
D000596:Amino Acids; D000469:Alkaline Phosphatase; D000252:Calcium-Transporting ATPases; D002118:Calcium