Influence of specific gamma-carboxyglutamic acid residues on the integrity of the calcium-dependent conformation of human protein C.

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Article

Influence of specific gamma-carboxyglutamic acid residues on the integrity of the calcium-dependent conformation of human protein C.

The Journal of biological chemistry - 25 Dec 1992

Zhang L, Castellino F J

Abstract excerpt

The concentration of Ca2+ that produced 50% of the saturable intrinsic fluorescence change (C50) of wild-type (wt) recombinant (r) human protein C (PC) was 0.40 mM. The C50 for Ca2+ increased < 2.5-fold for the following r-PC variants (Gla is gamma-carboxyglutamic acid): [Gla6-->Asp]r-PC, [Gla7-->Asp]r-PC, [Gla14-->Asp]r-PC, [Gla19-->Asp]r-PC, or [Gla25-->Asp]r-PC, and approximately 4-6-fold for [Gla20-->Asp]r-PC...

Topics

1-Carboxyglutamic Acid
Amino Acid Sequence
Antibodies, Monoclonal
Calcium
Cell Line
Genetic Variation
Humans
Kidney
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein C

Protein Conformation

Recombinant Proteins

Spectrometry, Fluorescence

Transfection

X-Ray Diffraction

Source

Open in PubMed

Identifiers

PMID: 1464619

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1464619-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Influence of specific gamma-carboxyglutamic acid residues on the integrity of the calcium-dependent conformation of human protein C.PMID 1464619Read ↗

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