Cargando…
Isolation and analysis of the mechanism of action of an inactivator of C4b in normal human serum
A complement regulatory principle, C4b inactivator, was isolated in a partially purified form from normal human serum. The C4b inactivator, a beta1-globulin with an approximate mol wt of 88,000 daltons, and which may be identical to C3b inactivator, cleaved C4b in free solution or on the surface of...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1975
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189755/ https://www.ncbi.nlm.nih.gov/pubmed/47888 |
Ejemplares similares
-
Human complement C3b inactivator: isolation, characterization, and demonstration of an absolute requirement for the serum protein beta1H for cleavage of C3b and C4b in solution
Publicado: (1977) -
A SPECIFIC INACTIVATOR OF MAMMALIAN C'4 ISOLATED FROM NURSE SHARK (Ginglymostoma cirratum) SERUM
por: Jensen, Joerg A.
Publicado: (1969) -
Human C4-binding protein. II. Role in proteolysis of C4b by C3b- inactivator
Publicado: (1978) -
OBSERVATIONS ON THROMBIN INACTIVATION BY HUMAN SERUM
por: Mihályi, Elemer
Publicado: (1953) -
The mechanism of action of the C3b inactivator (conglutinogen- activating factor) on its naturally occurring substrate, the major fragment of the third component of complement (C3b)
por: Gitlin, JD, et al.
Publicado: (1975)