نتایج جستجو برای: glanzmanns thrombasthenia

تعداد نتایج: 525  

Journal: :The Japanese Journal of Veterinary Science 1987

Journal: :Blood 1987
B S Coller U Seligsohn P A Little

A sensitive immunoblot technique for platelet glycoprotein IIIa (GPIIIa) was used to analyze the platelets of patients living in Israel who meet the diagnostic criteria for type I Glanzmann thrombasthenia. When reacted with solubilized normal platelets, a rabbit antiserum to GPIIIa identified a major band at molecular weight (mol wt) 90,000 and three additional minor bands at Mr 110,000, 81,000...

Journal: :iranian journal of blood and cancer 0
hemmati t farsinezhad a managhchi mr toogeh g faranoush m

background: activated normal platelets undergo many biochemical and morphological changes, some of which are apoptotic. platelet derived microparticles and shrinked platelets as hallmark of platelet activation and apoptosis disperse surfaces containing procoagulant activity around injured vessels and tissues. this study was conducted to determine microparticles formation and platelet shrinkage ...

Journal: :American Journal of Clinical Pathology 2008

Journal: :Expert Opinion on Orphan Drugs 2018

2005
Mary E. Russell Un Seligsohn Barry S. Coller Mark H. Ginsberg Paul Skoglund Thomas Quertermous

Glanzmann thrombasthenia is an autosomal recessive disorder of the platelet glycoproteins (GP) lIb and lila. These glycoproteins normally serve as receptors for other adhesive glycoproteins. including fibrinogen, von Willebrand factor, and fibronectin. Most patients affected by Glanzmann thrombasthenia have low levels of GPIIb and GPIIIa; however. the separate mechanisms responsible for the def...

Journal: :Blood 1988
S L Pfueller R A Bilston D Logan J M Gibson B G Firkin

The molecular nature of platelet receptors for quinine- and quinidine-dependent antiplatelet antibodies (Q.Ab and Qd.Ab) was studied by immunoblotting. One Q.Ab caused quinine-dependent IgG binding to platelet proteins with molecular weights (mol wts) of 174 Kd and 93 Kd and another to only a 93-Kd protein. A third Q.Ab caused binding to 174-, 140-, 93-, and 57-Kd proteins, while a fourth Q.Ab ...

Journal: :American Journal of Hematology 1992

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