Journal of Biological Chemistry · 1982 · 74 citations · 12 references
Life SciencesBiochemistryCell BiologyCell SignalingCellular MetabolismMembrane BiochemistryCell-surface LabelingCell-surface ReceptorsAdenosine TriphosphatasesBinding CapacityCell-surface Protein LabelingFractionationIndirect Immunofluorescence AssaySubcellular Fractionation
We have studied the cellular localization of human adenosine deaminase binding protein in human skin fibroblasts. The binding activity sediments with the membrane fractions in a subcellular fractionation, and anti-binding protein antiserum reacts with the cell surface of intact fibroblasts, as shown by indirect immunofluorescence. The surface of intact fibroblasts binds 125I-labeled adenosine deaminase with an apparent KD of 0.26 units/ml and a maximum binding capacity of 553 milliunits/mg of cell protein. This binding is inhibited by antibinding protein antiserum. We conclude that most, if not all, of the adenosine deaminase binding protein is located on the cell surface.
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Flora Katz, James E. Rothman, Vishwanath R. Lingappa et al. · Proceedings of the National Academy of Sciences · 1977 · 366 citations · Full text