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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Fernlund, P. Roepstorff, P. Stenflo, J. Drakenberg, T. |
| Abstract | Previous work has shown that the light chain of protein C, an anticoagulant plasma protein, contains an unusual amino acid [Fernlund, P. & Stenflo, J. (1982) J. Biol. Chem. 257, 12170-12179]. To determine the structure of this amino acid a heptapeptide, CMCys-Ile-X-Gly-Leu-Gly-Gly (residues 69-75 in the light chain), was isolated from enzymatic digests of the light chain. According to automatic Edman sequence analysis, 1H NMR spectroscopy, and mass spectrometry the heptapeptide had beta-hydroxyaspartic acid in its third position, which corresponds to position 71 in the light 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 approximately equal to 1 mol of beta-hydroxyaspartic acid per mol of protein. The function of this amino acid, which, to the best of our knowledge, has not been found previously in proteins, is unknown. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 7 |
| Volume Number | 80 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1983-05-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Aspartic Acid Analogs & Derivatives Blood Coagulation Factors Glycoproteins Amino Acid Sequence Animals Magnetic Resonance Spectroscopy Mass Spectrometry Peptide Fragments Protein C Vitamin K Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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