Andexanet-α/heparin interaction/rivaroxaban

2019 ◽  
Vol 1772 (1) ◽  
pp. 34-34
Keyword(s):  
Heparin Interaction

A Kinetic Study of Glucocorticoid-Heparin Interaction on the In Vivo DNA-Synthesis of Mouse Lymphatic Organs

Immunobiology ◽  
1980 ◽  
Vol 157 (4-5) ◽  
pp. 379-389
Author(s):  
E. Karczag ◽  
K. Kelemenics ◽  
I. Jókay ◽  
I. Földes
Keyword(s):  
Dna Synthesis ◽  
Kinetic Study ◽  
Heparin Interaction ◽  
Lymphatic Organs

scholarly journals Site-Specific Identification of an Aβ Fibril-Heparin Interaction Site by Using Solid-State NMR Spectroscopy

2012 ◽  
Vol 124 (52) ◽  
pp. 13317-13320
Author(s):  
Jillian Madine ◽  
Maya J. Pandya ◽  
Matthew R. Hicks ◽  
Alison Rodger ◽  
Edwin A. Yates ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Site Specific ◽  
Specific Identification ◽  
Interaction Site ◽  
Solid State Nmr Spectroscopy ◽  
Heparin Interaction

Heparin interaction

Reactions ◽  
1986 ◽  
Vol 153 (1) ◽  
pp. 8-9
Keyword(s):  
Heparin Interaction

Heparin interaction

1993 ◽  
Vol &NA; (440) ◽  
pp. 9
Author(s):  
&NA;
Keyword(s):  
Heparin Interaction

Ca2+ -heparin interaction investigated polarimetrically

1991 ◽  
Vol 19 (4) ◽  
pp. 391S-391S ◽  
Author(s):  
DAVID GRANT ◽  
COLIN F. MOFFAT ◽  
WILLIAM F. LONG ◽  
FRANK B. WILLIAMSON
Keyword(s):  
Heparin Interaction

Familial Overexpression of β Antithrombin Caused by an Asn135Thr Substitution

Blood ◽  
1999 ◽  
Vol 93 (12) ◽  
pp. 4242-4247
Author(s):  
T.A. Bayston ◽  
A. Tripodi ◽  
P.M. Mannucci ◽  
E. Thompson ◽  
H. Ireland ◽  
...  
Keyword(s):  
Direct Sequencing ◽  
Consensus Sequence ◽  
Wild Type ◽  
Antithrombin Deficiency ◽  
Free System ◽  
Heparin Interaction ◽  
A Cell ◽  
Variant Protein ◽  
Very High

We have investigated the basis of antithrombin deficiency in an asymptomatic individual (and family) with borderline levels (≈70% antigen and activity) of antithrombin. Direct sequencing of amplified DNA showed a mutation in codon 135, AAC to ACC, predicting a heterozygous Asn135Thr substitution. This substitution alters the predicted consensus sequence for glycosylation, Asn-X-Ser, adjacent to the heparin interaction site of antithrombin. The antithrombin isolated from plasma of the proband by heparin-Sepharose chromatography contained amounts of β antithrombin (the very high affinity fraction) greatly increased (≈20% to 30% of total) above the trace levels found in normals. Expression of the residue 135 variant in both a cell-free system and COS-7 cells confirmed altered glycosylation arising as a consequence of the mutation. Wild-type and variant protein were translated and exported from COS-7 cells with apparently equal efficiency, in contrast to the reduced level of variant observed in plasma of the affected individual. This case represents a novel cause of antithrombin deficiency, removal of glycosylation concensus sequence, and highlights the potentially important role of β antithrombin in regulating coagulation.

Sign in / Sign up

Export Citation Format

Share Document