Zobrazeno 1 - 9
of 9
pro vyhledávání: '"L. R. Paborsky"'
Autor:
V. S. Law, C. T. Mao, Anant K. Jain, Steven Coutre, S. Y. Mejza, L. R. Paborsky, Kyla E. Dunn, Lawrence L.K. Leung, Craig S. Gibbs, S. Y. Matsumura, W. X. Li, Manuel Tsiang
Publikováno v:
Nature. 378:413-416
AT sites of vascular injury, thrombin interacts with multiple procoagulant substrates1–6 to mediate both fibrin clotting and platelet aggregation. But upon binding to thrombomodulin on the vascular endothelium, thrombin instead activates protein C,
Publikováno v:
Journal of Biological Chemistry. 268:20808-20811
A new class of thrombin inhibitors based on sequence-specific single-stranded DNA oligonucleotides (thrombin aptamer) has recently been identified. The aptamer-binding site on thrombin was examined by a solid-phase plate binding assay and by chemical
Publikováno v:
Journal of Biological Chemistry. 266:4665-4668
The possible self-association of tissue factor molecules was investigated by treating cells expressing tissue factor with bifunctional cross-linking agents. The two reagents chosen were 3,3'-dithiobis(sulfosuccinimidylpropionate) and sulfosuccinimidy
Publikováno v:
The Journal of biological chemistry. 268(28)
A new class of thrombin inhibitors based on sequence-specific single-stranded DNA oligonucleotides (thrombin aptamer) has recently been identified. The aptamer-binding site on thrombin was examined by a solid-phase plate binding assay and by chemical
Publikováno v:
The Journal of biological chemistry. 266(32)
Full-length tissue factor (263 rTF) and three truncated forms have been expressed in human kidney 293 cells; 1) 243 rTF, which lacks the cytoplasmic tail, is fully functional in the chromogenic assay and has a specific activity comparable with that o
Publikováno v:
The Journal of biological chemistry. 266(8)
The possible self-association of tissue factor molecules was investigated by treating cells expressing tissue factor with bifunctional cross-linking agents. The two reagents chosen were 3,3'-dithiobis(sulfosuccinimidylpropionate) and sulfosuccinimidy
Autor:
L R, Paborsky, K M, Tate, R J, Harris, D G, Yansura, L, Band, G, McCray, C M, Gorman, D P, O'Brien, J Y, Chang, J R, Swartz
Publikováno v:
Biochemistry. 28:8072-8077
Tissue factor (TF) is a 263 amino acid membrane-bound procoagulant protein that serves as a cofactor for the serine protease factor VII (fVII). Recombinant human TF (rTF) produced in both human kidney 293 cells and Escherichia coli has been immunoaff
Publikováno v:
Journal of Biological Chemistry. 261:7958-7968
We describe the polypeptide structure and some of the catalytic properties of a DNA polymerase alpha.DNA primase complex that can be prepared from KB cells by immunoaffinity purification. The procedure is based on monoclonal antibodies that were rais
Publikováno v:
The Journal of biological chemistry. 261(17)
We describe the polypeptide structure and some of the catalytic properties of a DNA polymerase alpha.DNA primase complex that can be prepared from KB cells by immunoaffinity purification. The procedure is based on monoclonal antibodies that were rais