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ULTRASTRUCTURAL LOCALIZATION OF Mg++-DEPENDENT DINITROPHENOL-STIMULATED ADENOSINE TRIPHOSPHATASE IN HUMAN BLOOD PLATELETS
Author(s) -
Victor G. Vethamany,
Sydney S. Lazarus
Publication year - 1967
Publication title -
journal of histochemistry and cytochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.971
H-Index - 124
eISSN - 1551-5044
pISSN - 0022-1554
DOI - 10.1177/15.5.267
Subject(s) - adenosine triphosphatase , dinitrophenol , triphosphatase , 2,4 dinitrophenol , platelet , chemistry , enzyme , adenosine triphosphate , ultrastructure , biochemistry , mitochondrion , calcium , atpase , biophysics , biology , anatomy , organic chemistry , immunology
Fine structural localization of adenosine triphosphatase activity was studied in human platelets briefly fixed in cold formol calcium and then incubated in lead medium with added dinitrophenol. Under these conditions, the Mg ++ -dependent dinitrophenol-stimulated adenosine triphosphatase of platelet mitochondria was demonstrated, but neither granules nor plasma membrane showed enzyme activity.

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