1887

Abstract

Summary

Calcium-dependent binding of C-reactive protein (CRP) to was determined by enzyme-linked immunosorbent assay. A homogenate of young hyphae was fractionated by hydrophobic interaction chromatography followed by gel filtration. High CRP-binding activity was found in a fraction of mol. wt 500,000 which was characterised by strong binding to the hydrophobic column. Three fractions of less conspicuous CRP-binding activity were identified ( 500 000, 150 000 and 150 000–50 000 mol. wt respectively). In these four fractions, phosphorylcholine was detected by an anti-phosphorylcholine mouse hybridoma antibody. Some CRP-binding activity in fractions with low affinity for the hydrophobic column did not correspond closely with the presence of phosphorylcholine. It is suggested that C-reactive substance in is heterogeneous. The C-reactive substances did not correspond with fractions containing major antigens (470 000 and 250 000 mol. wt respectively) which elicit a strong immune response in man.

Loading

Article metrics loading...

/content/journal/jmm/10.1099/00222615-21-2-173
1986-03-01
2019-12-10
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/jmm/10.1099/00222615-21-2-173
Loading
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error