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CHARACTERIZATION OF THE ACID PHOSPHATASE ACTIVITY IN THE PLASMA MEMBRANE FRACTION FROM BABY HAMSTER KIDNEY CELLS (BHK21)
Author(s) -
GAHMBERG CARL G.,
SIMONS KAI
Publication year - 1970
Publication title -
acta pathologica microbiologica scandinavica section b microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0365-5563
DOI - 10.1111/j.1699-0463.1970.tb04327.x
Subject(s) - acid phosphatase , phosphatase , biochemistry , hamster , chemistry , membrane , phosphotransferase , enzyme , adenosine triphosphate , chromatography , biology , microbiology and biotechnology
We have studied the acid phosphatases in the plasma membrane fraction from baby hamster kidney cells (BHK21). The plasma membrane acid phosphatases utilized various monophosphates, including mononucleotides, and adenosine diphosphate but not adenosine triphosphate. They also had phosphotransferase activity with glycerol as acceptor. No requirement for magnesium was found. The acid phosphatases from the plasma membrane and lysosomal fractions were almost completely inhibited by fluoride and tartrate ions and to a smaller extent by sulphate ions. However the enzymes in the soluble fraction were much less sensitive to these inhibitors. In Triton disc electrophoresis the acid phosphatase banding pattern with 2‐glycerophosphate as substrate was found to be characteristic for the plasma membrane fraction. This pattern clearly differed from the banding patterns obtained with the lysosomal and soluble fractions.