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The first edition of this manual appeared in 1992 and was entitled ECAT Assay Procedures. It was the result of a unique cooperation between experts brought together by the European Concerted Action on Thrombosis and Disabilities (ECAT). The Concerted
This book offers a description of current and recently developed laboratory assays in the field of haemostasis and thrombosis. It is the result of a unique cooperation between experts from more than 60 institutes in 12 European countries, brought tog
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Autor:
F.R. Rosendaal, R.M. Bertina
Publikováno v:
New England Journal of Medicine. 338:1840-1841
Venous thrombosis is the obstruction of the circulation by clots that have been formed locally in the veins or have been released from a thrombus elsewhere. The usual sites of thrombus formation ar...
Publikováno v:
Biomedicine & Pharmacotherapy. 47:49
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 368:279-297
1. The concentration of specific oligomycin-binding sites in rat-liver mitochondria is 0.12 nmole/mg protein, whereas at least 10-times more oligomycin can be bound non-specifically. 2. The activity of oligomycin-inhibited processes in intact mitocho
Publikováno v:
Thrombosis and Haemostasis. 42:1296-1305
SummaryTwo spectrophotometric assays for prothrombin have been developed and compared with a one stage coagulant and an immunological assay. One of these assays (called the XAPC assay) uses a combination of factor Xa, phospholipid, Ca2+ and factor V
Publikováno v:
Thrombosis Research. 13:537-541
Autor:
Ria J. Boekhout-Mussert, J.J. Veltkamp, J. Dubbeldam, R.M. Bertina, Willy Van Der Marel-Van Nieuwkoop
Publikováno v:
Clinica Chimica Acta. 105:93-98
A new method is introduced for the rapid detection of vitamin K deficiency. The method is based on the direct measurement of the precursor factor II molecules that enter the blood in cases of vitamin K deficiency. The practical use of the new method
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 305:503-518
1. The fluorescence of aurovertin increases about 100-fold on binding to sub-mitochondrial particles. 2. The mitochondrial ATPase (F 1 ) binds one mole aurovertin/mole F 1 with a dissociation constant of 6·10 −8 M. 3. The fluorescence of mitochond