Results 91 to 97 of about 1,533 (97)

Limited Proteolysis of Complement Protein C3b by Regulatory Enzyme C3b Inactivator: Isolation and Characterization of a Biologically Active Fragment, C3d,g

The Journal of Biochemistry, 1985
Limited proteolysis of C3b by C3b inactivator (factor I) consists of a two-step reaction; rapid cleavage of C3b to yield a nicked C3b derivative, iC3b, and followed by slow cleavage of iC3b to yield two antigenically distinct fragments, C3c and C3d,g.
Tsukasa Seya, Shigeharu Nagasawa
openalex   +3 more sources

Regulatory proteins for the activated third and fourth components of complement (C3b and C4b) in mice. I. Isolation and characterization of factor H: the serum cofactor for the C3b/C4b inactivator (Factor I)

Journal of Immunological Methods, 1984
Factor H, purified from mouse EDTA-plasma using a 4-step procedure, consists of a single polypeptide chain of Mr 150,000 on SDS-PAGE. Mouse H (Hmo) was required for the cleavage of fluid-phase mouse C3b by mouse I (Imo). The final product of degradation of fluid-phase mouse C3b was iC3b, consisting of fragments of the alpha'-chain (alpha'-70, alpha'-43)
Taroh Kinoshita, Victor Nussenzweig
openalex   +3 more sources

Interaction of the fourth component of human complement, treated with amines, chaotropes or frozen-thawed (C4b-like C4), with C4 binding protein and cleavage by C3b/C4b inactivator

Molecular Immunology, 1982
I. von Zabern, Elyse Bloom, Valeria Chu, Irma Gigli   +3 more
openalex   +2 more sources

Some of the next articles are maybe not open access.

Related searches:

Factor I-dependent inactivation of human complement C4b of the classical pathway by C3b/C4b receptor (CR1, CD35) and membrane cofactor protein (MCP, CD46).

Journal of biochemistry, 1992
Proteolytic inactivation of C4b is a crucial step for regulation of the classical complement pathway. A plasma protease factor I and membrane cofactors, C3b/C4b receptor (CR1) and membrane cofactor protein (MCP), participate in the regulation of cell-bound C4b although the physiological potency of these cofactors remains unknown.
T, Masaki, M, Matsumoto, I, Nakanishi, R, Yasuda, T, Seya   +4 more
openaire   +2 more sources

Interaction of vaccinia virus complement control protein with human complement proteins: Factor I-mediated degradation of C3b to iC3b1 inactivates the alternative complement pathway

Molecular Immunology, 1998
Abstract Vaccinia virus complement control protein (VCP) is a virulence determinant of vaccinia virus that helps protect the virus from the complement attack of the host. To characterize the interaction of VCP with C3 and C4 and understand the mechanism by which VCP inactivates complement, we have expressed VCP in a yeast expression ...
A, Sahu, S N, Isaacs, A M, Soulika, J D, Lambris   +3 more
openaire   +2 more sources

[Functions and structure of complement inactivators in membrane proteins. 1). C3b/C4b receptor].

, 1988
Tsukasa Seya
openalex  

[Functions and structure of complement inactivators in membrane proteins. 1). C3b/C4b receptor].

Nihon rinsho. Japanese journal of clinical medicine, 1989
openaire   +1 more source