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Protein histidine phosphatase activity in rat liver and spinach leaves
Author(s) -
Matthews Harry R.,
MacKintosh Carol
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00353-b
Subject(s) - phosphatase , spinach , protein phosphatase 2 , histidine , biochemistry , acid phosphatase , cytosol , chemistry , enzyme , divalent , biology , organic chemistry
Whole cell extracts from rat liver or spinach leaves contain divalent ion‐independent protein histidine phosphatase activity due to phosphatases of the PP1/PP2A family. In the rat liver extract, almost all the activity was found in the PP1, PP2A 1 and PP2 2 peaks. In the spinach leaf extract, four phosphorylase phosphatase activity peaks were resolved — three containing PP1 and one containing PP2A — and all showed histidine phosphatase activity. Thus, protein histidine phosphatase activity is expressed in the cytosolic forms of protein phosphatases of the PP1/PP2A family in mammalian and plant cells.