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PMID: 6572939 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

beta-Hydroxyaspartic acid in vitamin K-dependent protein C.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 80 ·No. 7 ·1983-04-00 ·Pages 1802-6

Drakenberg T, Fernlund P, Roepstorff P, Stenflo J

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.

MeSH Terms
Amino Acid Sequence Animals Aspartic Acid/analogs & derivatives Blood Coagulation Factors Cattle Glycoproteins Magnetic Resonance Spectroscopy Mass Spectrometry Peptide Fragments/analysis Protein C Vitamin K
Chemicals
Blood Coagulation Factors Glycoproteins Peptide Fragments Protein C Vitamin K Aspartic Acid
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Drakenberg T
Fernlund P
Roepstorff P
Stenflo J
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27 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.80.7.1802
Published
1983-04-00
Pages
1802-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC393697
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.80.7.1802 PMC Full Text View journal details
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