Characterization of human red blood cell tyrosine kinase |
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| Authors: | F Phan-Dinh-Tuy J Henry A Kahn |
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| Affiliation: | 1. Canadian Blood Services, Centre for Innovation, Ottawa, Ontario, Canada;2. Canadian Blood Services, Centre for Innovation, Edmonton, Alberta, Canada;3. Canadian Blood Services, Cord Blood Bank and Stem Cell Manufacturing, Ottawa, Canada;4. University of Alberta, Department of Laboratory Medicine and Pathology, Edmonton, Alberta, Canada;5. University of Ottawa, Biochemistry, Microbiology and Immunology Department, Ottawa, Canada;1. Department of Radiation Oncology, USA;2. Laboratory of Signal Transduction, USA;3. Head and Neck Service, Department of Surgery, USA;4. Molecular Cytology Core Facility, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY, USA;5. Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA |
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| Abstract: | A new tyrosine kinase in human red blood cells has been characterized and partially purified. The major substrate was a protein of molecular weight 93 K which could be phosphorylated both in whole red blood cells incubated with inorganic [32P] orthophosphate and in ghost preparations incubated with [gamma 32P] ATP. This tyrosine kinase displayed an alkaline isoelectric pH (around 8.5), a molecular weight of 32-33 K and does not seem to be autophosphorylable. Some kinetics of the enzyme are reported. This red blood cell tyrosine kinase is unrelated to EGF and insulin or insulin-like receptor subunits. This enzyme may represent a novel class of tyrosine kinases. |
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