MALDI Imaging Mass Spectrometry Spatially Maps Age-Related Deamidation and Truncation of Human Lens Aquaporin-0
Author(s) -
Jamie L. Wenke,
Kristie L. Rose,
Jeffrey M. Spraggins,
Kevin L. Schey
Publication year - 2015
Publication title -
investigative ophthalmology and visual science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.935
H-Index - 218
eISSN - 1552-5783
pISSN - 0146-0404
DOI - 10.1167/iovs.15-18117
Subject(s) - deamidation , chemistry , mass spectrometry , peptide , tandem mass spectrometry , chromatography , biochemistry , enzyme
To spatially map human lens Aquaporin-0 (AQP0) protein modifications, including lipidation, truncation, and deamidation, from birth through middle age using matrix-assisted laser desorption ionization (MALDI) imaging mass spectrometry (IMS).
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