Polycystin-1: immunoaffinity isolation and characterisation by mass spectrometry |
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Authors: | Malhas A N Abuknesha R A Price R G |
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Affiliation: | Department of Biochemistry, School of Life Sciences, King's College London, London SE1 9NN, UK. ashraf.malhas@kcl.ac.uk |
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Abstract: | Polycystin-1 is a putative 460 kDa membrane protein with a unique structure and is possibly representative of a new family of proteins. Its structure suggests an involvement in cell signalling and cell-matrix interactions. The amino acid sequence of polycystin-1 has to date been predicted from its gene sequence. This, to our knowledge, is the first report of the isolation and analysis of polycystin-1 at the protein level using mass spectrometry to confirm its predicted structure. The availability of purified polycystin-1 will allow a new approach to unravelling the complexity of the cell-cell and cell-matrix interactions of this large molecule in normal cells and its perturbation in disease. |
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