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FEBS Lett. 1987 Sep 28;222(1):129-34.

Identification of erythro-beta-hydroxyasparagine in the EGF-like domain of human C1r.

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Département de Recherches Fondamentales, Unité INSERM 238, CEN-Grenoble 85 X, France.


Previous studies [(1987) Biochem. J. 241, 711-720] have shown that position 150 of human C1r is occupied by a modified amino acid that, after acid hydrolysis, yields erythro-beta-hydroxyaspartic acid. In view of further investigations on the nature of this residue, peptide CN1a T8/T9 TL8 (positions 147-155) was isolated from C1r A chain by CNBr cleavage followed by enzymatic cleavages by trypsin and thermolysin. Amino acid analysis, sequential Edman degradation and FAB-MS of this peptide indicate that the residue at position 150 is an erythro-beta-hydroxyasparagine resulting from post-translational hydroxylation of asparagine.

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