The human red cell acid phosphatase is a phosphotyrosine protein phosphatase which dephosphorylates the membrane protein band 3 |
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| Authors: | P Boivin C Galand |
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| Institution: | 1. Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA;2. Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA;3. Thermo Fisher Scientific GmbH, Bremen, Germany;4. National Center for Quantitative Biology of Complex Systems, Madison, Wisconsin, USA;5. Morgridge Institute for Research, Madison, Wisconsin, USA;6. Thermo Fisher Scientific, San Jose, California, USA;1. Department Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany;2. Thermo Fisher Scientific (GmbH), Bremen, Germany;3. Department Clinical Proteomics, NNF Center for Protein Research, University of Copenhagen, Copenhagen, Denmark;4. Department Computational Systems Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany;5. Functional Proteomics, Jena University Hospital, Jena, Germany;1. Department of Anthropology, University of Delhi, Delhi, 110007, India;2. National Institute of Epidemiology Social and Behavioural Sciences, Chennai, Tamilnadu, 600077, India |
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| Abstract: | Human red cell cytosol acid phosphatase activity is supported by a main enzyme which can be extracted by DEAE and phosphocellulose chromatography. It uses pNPP as a substrate and is a protein phosphatase specific to phosphotyrosine. It dephosphorylates the tyrosine-phosphorylated cytosolic fragment of membrane protein 3. When taken together, these results suggest that the physiological role of red cell acid phosphatase is the FB3 phosphotyrosine dephosphorylation. Whatever it may be phosphotyrosine protein phosphatase activity is the first role of red cell acid phosphatase to be demonstrated. |
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