Prolyl 3-hydroxylation at Pro986 in the α2(V) collagen chain.
- Erica P. Homan (249068)
- Caressa Lietman (513876)
- Ingo Grafe (513877)
- Jennifer Lennington (249063)
- Roy Morello (249088)
- Dobrawa Napierala (513878)
- Ming-Ming Jiang (249071)
- Elda M. Munivez (513879)
- Brian Dawson (513880)
- Terry K. Bertin (513881)
- Yuqing Chen (231681)
- Rhonald Lua (207266)
- Olivier Lichtarge (22747)
- John Hicks (513882)
- Mary Ann Weis (513883)
- David Eyre (920)
- Brendan H. L. Lee (513884)
Publication date
January 2014
DOIAbstract
<p>Mass spectral analysis of Pro986 hydroxylation in tryptic peptides from the α2(V) chain of bone from <i>Lepre1<sup>+/+</sup></i> and <i>Lepre1<sup>H662A/H662A</sup></i> mice (A and B respectively) shows a marked reduction in hydroxylation at this site. The MS/MS fragmentation patterns shown in C and D identified the 765.8<sup>2+</sup> peptide and its 3-hydroxylated version 773.9<sup>2+</sup>. A portion (40%) of the latter ion was also found by MS/MS to be contributed by a version lacking 3-Hyp but containing 4-Hyp at P978 (taken into account in the 3-Hyp quantitation).</p
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