Prothrombin's calcium ion binding site, carbon-13 nuclear magnetic resonance studies

K. A. Koehler, D. A. Gabriel, R. G. Hiskey, R. L. Lundblad, H. R. Roberts, G. L. Nelsestuen

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Carbon-13 nuclear magnetic resonance (NMR) spectra are reported for vitamin K-dependent peptide (VKP) and profragment-1, both derived from bovine prothrombin. These prothrombin fragments contain γ-carboxyglutamic acid (GLA) residues and it is possible to assign those resonances in the VKP spectrum due to this entity based on comparison with methyl malonic acid and synthetic γ-carboxyglutamic acid derivatives (1). At neutral pH the following assignments (chemical shifts are reported in PPM relative to tetramethylsilane) can be made: carboxyl carbons, 175.8; α-carbon, 58.5; β-carbon, 32.5; γ-carbon, 52.3. These resonance positions depend significantly on pH.

Original languageEnglish (US)
Pages (from-to)871-877
Number of pages7
JournalThrombosis Research
Volume7
Issue number6
DOIs
StatePublished - Dec 1975

Fingerprint Dive into the research topics of 'Prothrombin's calcium ion binding site, carbon-13 nuclear magnetic resonance studies'. Together they form a unique fingerprint.

Cite this