Polycystin-1: immunoaffinity isolation and characterisation by mass spectrometry.
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 g...
Main Authors: | , , |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2001
|
_version_ | 1797058864100671488 |
---|---|
author | Malhas, A Abuknesha, R Price, R |
author_facet | Malhas, A Abuknesha, R Price, R |
author_sort | Malhas, A |
collection | OXFORD |
description | 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. |
first_indexed | 2024-03-06T19:56:23Z |
format | Journal article |
id | oxford-uuid:25be90f8-8b87-4f49-95c1-78c0de343a2b |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-06T19:56:23Z |
publishDate | 2001 |
record_format | dspace |
spelling | oxford-uuid:25be90f8-8b87-4f49-95c1-78c0de343a2b2022-03-26T11:57:15ZPolycystin-1: immunoaffinity isolation and characterisation by mass spectrometry.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:25be90f8-8b87-4f49-95c1-78c0de343a2bEnglishSymplectic Elements at Oxford2001Malhas, AAbuknesha, RPrice, RPolycystin-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. |
spellingShingle | Malhas, A Abuknesha, R Price, R Polycystin-1: immunoaffinity isolation and characterisation by mass spectrometry. |
title | Polycystin-1: immunoaffinity isolation and characterisation by mass spectrometry. |
title_full | Polycystin-1: immunoaffinity isolation and characterisation by mass spectrometry. |
title_fullStr | Polycystin-1: immunoaffinity isolation and characterisation by mass spectrometry. |
title_full_unstemmed | Polycystin-1: immunoaffinity isolation and characterisation by mass spectrometry. |
title_short | Polycystin-1: immunoaffinity isolation and characterisation by mass spectrometry. |
title_sort | polycystin 1 immunoaffinity isolation and characterisation by mass spectrometry |
work_keys_str_mv | AT malhasa polycystin1immunoaffinityisolationandcharacterisationbymassspectrometry AT abukneshar polycystin1immunoaffinityisolationandcharacterisationbymassspectrometry AT pricer polycystin1immunoaffinityisolationandcharacterisationbymassspectrometry |