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J. Biol. Chem., Vol. 269, Issue 17, 12494-12502, Apr, 1994
LR Miesbauer, X Zhou, Z Yang, Z Yang, Y Sun, DL Smith and JB Smith
Post-translational modifications of the water-soluble human lens
crystallins from young adult donors were identified and located using
electrospray ionization mass spectrometric analysis of the intact proteins
and fast atom bombardment mass spectrometry of enzymatic digests. Peptides
corresponding to all of the sequences of alpha A-, alpha B-, and beta
B2-crystallins were found, permitting the entire sequences to be searched
for modifications. The major portions of these three crystallins were not
modified. Modifications of alpha A- crystallin that were detected included
2 phosphorylated Ser residues (1 of which appears to be unique to human
lenses), deamidation at some Gln and Asn residues, a disulfide bond between
Cys-131 and Cys-142, and loss of the COOH-terminal Ser residue. Three
phosphorylated Ser residues, but no deamidation, were found in alpha
B-crystallin. The molecular weights of neither the intact protein nor the
peptides in the enzymatic digests indicated any post-translational
modification of the principal beta-crystallin, beta B2. The molecular
weights of the other beta- and gamma-crystallins for which sequences have
been published suggested the presence of post-translational modifications
or errors in the published sequences. Although enough peptides were found
to establish the presence of specific proteins, peptides corresponding to
all portions of these proteins were not found, and elucidation of these
structures is not yet complete. This mass spectrometric characterization of
the total water-soluble proteins from normal young adult lenses provides a
reference data base for future investigations of the modifications present
in aged and cataractous lenses.
Post-translational modifications of water-soluble human lens crystallins from young adults
Department of Medicinal Chemistry and Pharmacognosy, Purdue University, West Lafayette, Indiana 47907.
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