beta-Hydroxyaspartic acid in vitamin K-dependent protein C.
- 1 April 1983
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 80 (7) , 1802-1806
- https://doi.org/10.1073/pnas.80.7.1802
Abstract
The L chain of protein C, an anticoagulant plasma protein, apparently contains an unusual amino acid. To determine the structure of this amino acid a heptapeptide, CMCys-Ile-X-Gly-Leu-Gly-Gly (residues 69-75 in the L chain), was isolated from enzymatic digests of the L chain. According to automatic Edman sequence analysis, 1H NMR spectroscopy and mass spectrometry, the heptapeptide had .beta.-hydroxyaspartic acid in its 3rd position, which corresponds to position 71 in the L chain of protein C. Analysis of acid and aminopeptidase M hydrolysates of the heptapeptide showed the .beta.-hydroxyaspartic acid to be the erythro form. Acid hydrolysis of protein C released .apprxeq. 1 mol of .beta.-hydroxyaspartic acid/mol of protein. The function of this amino acid, which was not found previously in proteins, is unknown.This publication has 27 references indexed in Scilit:
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