Zobrazeno 1 - 10
of 49
pro vyhledávání: '"V H, Donaldson"'
Publikováno v:
Blood. 75:911-921
Activated high molecular weight Hageman factor (75 Kd) and Hageman factor carboxy-terminal fragments both formed complexes with purified C1(-)-inhibitor, but the Hageman factor fragments appeared to have a higher affinity for the C1(-)-inhibitor than
Publikováno v:
Proceedings of the Association of American Physicians. 110(2)
A highly purified protein from lysates of human umbilical vein endothelial cells (HUVECs) inhibited the activation of factor XII [Hageman factor (HF)] and removed factor XIIa from an activating surface, thus impairing HF-dependent coagulation and kin
Publikováno v:
The Journal of laboratory and clinical medicine. 127(2)
An autoantibody to C1-inhibitor produced a clinical disorder resembling that of patients with hereditary angioneurotic edema. The antibody could not interact with C1-inhibitor after exposure to synthetic peptides representing the primary structure of
Publikováno v:
Behring Institute Mitteilungen. (93)
Autor:
V H, Donaldson, M W, Falconieri
Publikováno v:
Journal of immunological methods. 157(1-2)
Human C1- inhibitor can be rapidly purified by the affinity chromatography procedure described by Pilatte and his associates (1989), but the inhibitor so purified breaks down during storage or is in a cleaved form when initially purified. By adding a
Autor:
V H, Donaldson
Publikováno v:
The Journal of laboratory and clinical medicine. 121(1)
Autor:
V H, Donaldson, J J, Bissler
Publikováno v:
The Journal of laboratory and clinical medicine. 119(4)
Publikováno v:
The Journal of laboratory and clinical medicine. 119(4)
A patient with severe acquired angioneurotic edema had essentially no C1- inhibitor activity in his serum and nearly died of cardiopulmonary arrest during an acute episode of facial, oral, and pharyngeal edema. This patient had an antibody directed a
Publikováno v:
Journal of Biological Chemistry. 259:8522-8528
Autor:
Karen Skriver, Elzbieta Radziejewska, Jean A. Marrinan, Susan Clark Bock, B Wiman, R L Eddy, E Nielsen, Robert Huber, V H Donaldson, H C Thøgersen
Publikováno v:
Biochemistry. 25:4292-4301
The primary structure of human C1 inhibitor was determined by peptide and DNA sequencing. The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulati