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Tyrosine protein kinase activity in normal and leukaemic human blood cells
Author(s) -
Punt C. J. A.,
Rijksen G.,
Vlug A. M. C.,
Dekker A. W.,
Staal G. E. J.
Publication year - 1989
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1989.tb00219.x
Subject(s) - tyrosine , cytosol , cell , myeloid , biochemistry , biology , microbiology and biotechnology , chemistry , immunology , enzyme
Summary. Tyrosine protein kinase (TPK) activity was measured in subcellular fractions of normal granulocytes, lymphocytes and monocytes, and acute and chronic myeloid and lymphoid leukaemic cells. Of several tested tyrosine‐containing substrates, poly (glutamic acid: tyrosine = 4:1) (S 1 ) proved to be the best synthetic substrate. High cytosolic TPK activity was found in every cell type. Different TPKs may exist in various cell fractions, as was indicated by the difference in K m values for S 1 in cell fractions of normal granulocytes and lymphocytes. No significant difference was found in total TPK activity between normal and leukaemic cells, indicating that total TPK activity is not related to the leukaemic process itself. A highly significant difference was found in membrane fractions in normal granulocytes and M 1 –M 2 AML cells versus normal monocytes and M 1 –M 5 AML cells, suggesting an association between TPK activity and monocytic differentiation in these cell fractions.