@inbook{0d2bb7decf434e529870078b9d1d16e3,
title = "Identification of tyrosine O Sulfated proteins in cow retina and the 661W cell line",
abstract = "Lack of tyrosine O Sulfation compromises both rod and cone electroretinographic responses emphasizing the importance of this post-translational modification for vision. To identify tyrosine sulfated proteins in retina, cow retinal lysates were subjected to immunoaffinity purification using an anti-sulfotyrosine antibody. The tyrosine sulfated proteins were eluted from the column using a sulfotyrosine pentapeptide and identified using mass spectrometry. Similarly, tyrosine sulfated proteins secreted by the 661W cell line were identified. Proteins identified were vitronectin, fibronectin, fibulin 2, nidogen, collagen V alpha 2, complement component 3 and C4 and fibrinogen beta. All proteins were subjected to analysis by {\textquoteleft}Sulfinator{\textquoteright} to determine potential sulfated tyrosines.",
keywords = "661W, PSG2, Posttranslational modification, Retina, Tyrosine sulfation",
author = "Yogita Kanan and Al-Ubaidi, {Muayyad R.}",
note = "Funding Information: This study was supported by grants from Oklahoma Center for Advancement of Science and Technology (OCAST to YK), Foundation Fighting Blindness (MRA), the National Eye Institute EY018137 (MRA) and a P30EY021725. The funders had no role in design, collection and analysis of data, decision to publish, or manuscript preparation. Publisher Copyright: {\textcopyright} Springer International Publishing Switzerland 2016.",
year = "2016",
month = oct,
day = "1",
doi = "10.1007/978-3-319-17121-0_86",
language = "English (US)",
series = "Advances in Experimental Medicine and Biology",
publisher = "Springer New York LLC",
pages = "649--654",
booktitle = "Advances in Experimental Medicine and Biology",
}