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Similarities between alkaline phosphatase and CA 2+ ATPase activities in HeLa cells
Author(s) -
Brahmacupta Prem,
Melnykovych George
Publication year - 1980
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041050206
Subject(s) - alkaline phosphatase , enzyme , atpase , hela , acid phosphatase , biochemistry , chemistry , egta , phosphatase , phenylalanine , enzyme assay , microbiology and biotechnology , biology , calcium , cell , amino acid , organic chemistry
Parallel changes in the enzyme activities of Ca 2+ 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°C, 60°C, and 65°C) resulted in a loss of both enzyme activities. Both alkaline phosphatase and Ca 2+ ATPase, when treated with EGTA, required Ca 2+ 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.