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Polycystin‐1: immunoaffinity isolation and characterisation by mass spectrometry
Author(s) -
Malhas Ashraf N.,
Abuknesha Ramadan A.,
Price Robert G.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02842-3
Subject(s) - isolation (microbiology) , mass spectrometry , chromatography , chemistry , biology , bioinformatics
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.