Phosphorylation and glycosylation of bovine lens MP20.

@article{Ervin2005PhosphorylationAG,
  title={Phosphorylation and glycosylation of bovine lens MP20.},
  author={Lisa A Ervin and Lauren Ball and Rosalie K. Crouch and Kevin L. Schey},
  journal={Investigative ophthalmology & visual science},
  year={2005},
  volume={46 2},
  pages={627-35}
}
PURPOSE Membrane protein 20 (MP20) is the second most abundant integral membrane protein in the lens, yet little is known about its function and post-translational modifications. The purpose of this work was the determination of the primary protein structure of MP20 and the types and sites of in vivo modifications. METHODS Bovine MP20 was isolated by anion exchange chromatography or SDS-PAGE followed by digestion with cyanogen bromide (CNBr) or trypsin. The total membrane protein fraction was… CONTINUE READING

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The CNBr and trypsin peptides were analyzed by liquid chromatography - tandem mass spectrometry ( LC - MS / MS ) and matrix - assisted laser desorption ionization ( MALDI ) mass spectrometry .
The CNBr and trypsin peptides were analyzed by liquid chromatography - tandem mass spectrometry ( LC - MS / MS ) and matrix - assisted laser desorption ionization ( MALDI ) mass spectrometry .
The CNBr and trypsin peptides were analyzed by liquid chromatography - tandem mass spectrometry ( LC - MS / MS ) and matrix - assisted laser desorption ionization ( MALDI ) mass spectrometry .
The CNBr and trypsin peptides were analyzed by liquid chromatography - tandem mass spectrometry ( LC - MS / MS ) and matrix - assisted laser desorption ionization ( MALDI ) mass spectrometry .
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