Crossref journal-article
Wiley
FEBS Letters (311)
Abstract

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‐β‐hydroxyaspartic acid. In view of further investigations on the nature of this residue, peptide CN1a T8/T9 TL8 (positions 147–155) was isolated from Cr 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‐β‐hydroxyasparagine resulting from post‐translational hydroxylation of asparagine.

Bibliography

Arlaud, G. J., Van Dorsselaer, A., Bell, A., Mancini, M., Aude, C., & Gagnon, J. (1987). Identification of erythro‐β‐hydroxyasparagine in the EGF‐like domain of human C1r. FEBS Letters, 222(1), 129–134. Portico.

Authors 6
  1. Gérard J. Arlaud (first)
  2. Alain Van Dorsselaer (additional)
  3. Alex Bell (additional)
  4. Michael Mancini (additional)
  5. Catherine Aude (additional)
  6. Jean Gagnon (additional)
Dates
Type When
Created 23 years, 1 month ago (July 25, 2002, 3:45 a.m.)
Deposited 1 year, 11 months ago (Sept. 15, 2023, 11:25 p.m.)
Indexed 1 year, 7 months ago (Jan. 18, 2024, 9:26 a.m.)
Issued 37 years, 11 months ago (Sept. 28, 1987)
Published 37 years, 11 months ago (Sept. 28, 1987)
Published Online 23 years, 10 months ago (Oct. 19, 2001)
Published Print 37 years, 11 months ago (Sept. 28, 1987)
Funders 0

None

@article{Arlaud_1987, title={Identification of erythro‐β‐hydroxyasparagine in the EGF‐like domain of human C1r}, volume={222}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/0014-5793(87)80205-3}, DOI={10.1016/0014-5793(87)80205-3}, number={1}, journal={FEBS Letters}, publisher={Wiley}, author={Arlaud, Gérard J. and Van Dorsselaer, Alain and Bell, Alex and Mancini, Michael and Aude, Catherine and Gagnon, Jean}, year={1987}, month=sep, pages={129–134} }