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.
References
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{'key': 'e_1_2_1_25_1', 'first-page': '826', 'volume': '39', 'author': 'Kamboh M.I.', 'year': '1986', 'journal-title': 'Am. J. Hum. Genet.'}
/ Am. J. Hum. Genet. by Kamboh M.I. (1986)
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) |
@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} }