Phosphopeptides and γ-carboxyglutamic acid-containing peptides in calcified turkey tendon: Their absence in uncalcified tendon

1979 ◽  
Vol 27 (1) ◽  
pp. 281-284 ◽  
Author(s):  
Melvin J. Glimcher ◽  
Diane Brickley-Parsons ◽  
Dora Kossiva
Keyword(s):  
Carboxyglutamic Acid ◽  
Turkey Tendon

scholarly journals Proteolytic formation and properties of gamma-carboxyglutamic acid-domainless protein C.

1983 ◽  
Vol 258 (9) ◽  
pp. 5548-5553
Author(s):  
N L Esmon ◽  
L E DeBault ◽  
C T Esmon
Keyword(s):  
Protein C ◽  
Carboxyglutamic Acid

Terbium ion binding to a synthetic .gamma.-carboxyglutamic acid containing heptapeptide corresponding to bovine prothrombin residues 17-23

1986 ◽  
Vol 25 (25) ◽  
pp. 4503-4506 ◽  
Author(s):  
Henry C. Marsh ◽  
Randal A. Hoke ◽  
David W. Deerfield ◽  
Lee G. Pedersen ◽  
Richard G. Hiskey ◽  
...  
Keyword(s):  
Ion Binding ◽  
Carboxyglutamic Acid ◽  
Terbium Ion

scholarly journals Studies on Ca(II) binding to gamma-carboxyglutamic acid. Use of thermal decarboxylation to probe metal ion/gamma-carboxyglutamic acid interactions.

1988 ◽  
Vol 263 (3) ◽  
pp. 1358-1363
Author(s):  
M R Lewis ◽  
D W Deerfield ◽  
R A Hoke ◽  
K A Koehler ◽  
L G Pedersen ◽  
...  
Keyword(s):  
Metal Ion ◽  
Carboxyglutamic Acid ◽  
Thermal Decarboxylation

Purification and Characterization of Factor VII Inhibitor Found in a Patient with Life Threatening Bleeding

2000 ◽  
Vol 83 (01) ◽  
pp. 60-64 ◽  
Author(s):  
Seiji Miyamoto ◽  
Atsushi Iwasa ◽  
Masao Ishii ◽  
Kenji Okajima ◽  
Yu-ichi Kamikubo
Keyword(s):  
Light Chain ◽  
Calcium Ion ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Vii ◽  
Immunoblotting Analysis ◽  
Calcium Dependent ◽  
Sds Page ◽  
Carboxyglutamic Acid ◽  
Life Threatening ◽  
Gla Domain

SummaryWe recently observed a patient with acquired inhibitor-induced F.VII deficiency whose plasma level of F.VII was < 1.0%. However, the biochemical nature of the inhibitor has not yet been clarified. In the present study, we purified the F.VII inhibitor from the patient’s plasma by using activated F.VII (F.VIIa)-conjugated gel and characterized the inhibitor. The results showed that the inhibitor comprised two kinds of antibodies: one was eluted with EDTA (antibody 1) and the other with glycine-HCl buffer (pH 2.3) (antibody 2) from the F.VIIa affinity gel. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting analysis of these inhibitors demonstrated that both antibodies had features of immunoglobulin G1 (IgG1) with κ and λ-light chains. Antibody 1 bound to the immobilized F.VIIa with a high affinity in the presence of calcium ion, while antibody 2 bound to the F.VIIa very weakly and the binding was independent of calcium ion. Immunoblotting analysis demonstrated that antibody 1 bound to the light chain of F.VIIa after reduction with 2-mercaptoethanol, while it did not react with either the γ carboxyglutamic acid (Gla)-domainless light chain of F.VIIa or the heavy chain with the protease domain. Antibody 1 markedly inhibited the activity of tissue factor-F.VIIa complex. Based on these observations, it is suggested that F.VIIa autoantibody (antibody 1) recognizes the calcium-dependent conformation within or near the Gla domain and inhibits F.VIIa activity by interacting with the light chain.

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