Zobrazeno 1 - 8
of 8
pro vyhledávání: '"R J, Jenny"'
Publikováno v:
Blood. 81:704-719
Platelet activation leads to the incorporation of 32[PO4(2-)] into bovine coagulation factor Va and recombinant human factor VIII. In the presence of the soluble fraction from thrombin-activated platelets and (gamma-32P) adenosine triphosphate, radio
Publikováno v:
Methods in enzymology. 222
Publikováno v:
The Journal of biological chemistry. 265(35)
Coagulation factor Va is a cofactor which combines with the serine protease factor Xa on a phospholipid surface to form the prothrombinase complex. The phospholipid-binding domain of bovine factor Va has been reported to be located on the light chain
Publikováno v:
Blood Coagulation & Fibrinolysis. 9:674
Publikováno v:
Blood. 67:1583-1590
Monoclonal antibodies to human protein S have been prepared using established hybridoma technology. One antibody was isolated that binds protein S only when Ca2+ is present; others bind antigen equally well in the presence or absence of EDTA. Other a
Autor:
R. J. Jenny, U. Bolleter
Publikováno v:
Practical Experiences with Flow-Induced Vibrations ISBN: 9783642815300
Practical Experiences with Flow-Induced Vibrations
Practical Experiences with Flow-Induced Vibrations
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4ff0d33624b08d06791f579e043fa488
https://doi.org/10.1007/978-3-642-81528-7_27
https://doi.org/10.1007/978-3-642-81528-7_27
Publikováno v:
The Journal of nutrition. 118(11)
The relative amount of L-arginine:glycine amidinotransferase (transamidinase) protein in kidneys from rats fed a complete purified diet with and without the addition of creatine and/or glycine was determined by a monoclonal antibody-immunosorbent inh
Autor:
R J, Jenny, K G, Mann
Publikováno v:
Bailliere's clinical haematology. 2(4)
The relative abundance of factor V, factor X and prothrombin has enabled detailed analyses of the prothrombinase complex. Determination of the primary structure for factor V has provided the basis for examination of structure-function relationships.