Abstract
The primary structure and posttranslational modifications of rabbit lens α-crystallins were examined using electrospray ionization mass spectrometry to determine the molecular weights of the intact proteins and fast atom bombardment mass spectrometry to analyze proteolytic digests of the αA- and αB-crystallins. The previously determined primary structure of αA-crystallin was confirmed. Posttranslational modifications detected included one phosphorylation site and the presence of a truncated form minus the five C-terminal residues. The previously undetermined amino acid sequence of rabbit αB-crystallin was determined to be the same as the bovine αB-crystallin sequence except at three residues: Thr 40, Thr 132, and Pro 153. Rabbit αB-crystallin showed evidence of phosphorylation at the same three sites as bovine αB-crystallin. The molecular weights of the intact proteins indicated that any one molecule had a maximum of two phosphorylations. Also, there was a truncated form which did not include the five C-terminal residues.
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Parveen, R., Smith, J.B., Sun, Y. et al. Primary structure of rabbit lens α-crystallins. J Protein Chem 12, 93–101 (1993). https://doi.org/10.1007/BF01024920
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DOI: https://doi.org/10.1007/BF01024920