𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Complement activation by IgG immobilized on methylated silicon

✍ Scribed by Tengvall, Pentti ;Askendal, Agneta ;Lundstr�m, Ingemar


Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
785 KB
Volume
31
Category
Article
ISSN
0021-9304

No coin nor oath required. For personal study only.

✦ Synopsis


Activation of the complement system by immobilized IgG on methylated silicon was studied by ellipsometry/antibody-, ELISA-, and RIA techniques after exposure to human serum at 37°C for up to 1 h. The IgG-covered surfaces rapidly activated the complement system and the combined results suggest an initial classical pathway activation. Complement factor l q (Clq) and IgG were antibody-detectable on the surfaces for serum incubations up to 5 min but not thereafter. Anti-C3c and anti-properdin bound to the surfaces at all serum incubation times. Experiments with '=I-IgG preadsorbed to surfaces, or added to normal-, EGTA-, and EDTAsera, showed that IgG was not displaced from the protein film by serum.


📜 SIMILAR VOLUMES


Temporal studies on the deposition of co
✍ Tengvall, Pentti ;Askendal, Agneta ;Lundstr�m, Ingemar 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 311 KB

The temporal deposition of selected complement proteins from human serum onto immobilized human colostrum immunoglobulin (Ig)A and human IgG on hydrophobic silicon was studied by ellipsometry-antibody techniques after incubations at 37°C for up to 1 h. In parallel experiments the serum soluble iC3b,

HUMAN COMPLEMENT ACTIVATION BY SELF-ASSO
✍ Paul B. Brown; Francis A. Nardella; Mart Mannik 📂 Article 📅 1982 🏛 John Wiley and Sons 🌐 English ⚖ 658 KB

## Abstract IgG rheumatoid factors (IgG–RFs) undergo concentration‐dependent self‐association into dimers and higher polymers, as previously reported. The interactions of purified IgG–RF from the plasma of 3 patients with rheumatoid arthritis, with guinea pig and human complement were studied. Self