PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 321155

Haemolytic assays in agarose plates for components of the classical complement pathway: interference by the alternative pathway.

A Martin·P J Lachmann
View original source ↗Export metadata ↓

Abstract

It has been observed that when serum C6 is measured by the haemolytic radial diffusion technique a heat labile factor limits the size of the haemolytic rings. This reduction is haemolysis has been shown to be due to alternative pathway activation of C6 in the agarose plate; and that the heat labile factor is Factor B of the alternative pathway. This phenomenon is of practical importance when assaying for C6; however, it does not explain the observations of a C6 inactivator reported by Nelson & Biro (1968).

Explore related subjects

Antigen-Antibody ComplexComplement C5Complement C6Complement C7Complement System ProteinsHemolytic Plaque TechniqueHot TemperatureHumansSepharoseJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

A Martin, P J Lachmann. 1977. Haemolytic assays in agarose plates for components of the classical complement pathway: interference by the alternative pathway.. https://pubmed.ncbi.nlm.nih.gov/321155/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed1979

Immune complexes and the evolution of Lyme arthritis. Dissemination and localization of abnormal C1q binding activity.

In a prospective study of 78 patients with Lyme arthritis, abnormal serum C1q binding activity was present at the initial onset of erythema chronicum migrans in nearly all cases. The abnormal binding persisted in patients with subsequent nerve or heart involvement. In contrast, among those with only subsequent arthritis, it usually disappeared within three months (P = 0.018). However, in the synovial fluid of affected joints, abnormal binding was uniformly present, and always to a greater extent than in the circulation. The abnormally reactive material behaved like antigen-antibody complexes. It had a density of 19S or greater, dissociated below pH 4.2, and lacked antiglobulin activity. Cryoprecipitates containing immunoglobulin were good but insensitive predictors of its presence, but immune complexes themselves did not seem primarily responsible for cryoprecipitability. Thus, as judged by C1q binding, immune complexes remain disseminated in certain patients with Lyme arthritis but localize to joints in others.

Antigen-Antibody Complex↗