Loading…

Effect of Antiserum on Maltase from Intestinal Microvillous Membranes of Ascaris suum

This study is based on the premise that the nematode gut is the target of host-immune responses and is designed to test the hypothesis that antibodies reacting with antigenic sites on the surface of this organ interfere with its normal function. Ascaris suum was used as a model to investigate effect...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of parasitology 1974-02, Vol.60 (1), p.110-116
Main Authors: Gentner, Harry W., Castro, G. A.
Format: Article
Language:English
Subjects:
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:This study is based on the premise that the nematode gut is the target of host-immune responses and is designed to test the hypothesis that antibodies reacting with antigenic sites on the surface of this organ interfere with its normal function. Ascaris suum was used as a model to investigate effects of antibodies on the digestion of maltose. Specific experiments involved (1) the isolation of ascaris intestinal brush border, (2) the development of agglutination and precipitin tests for antibodies to brush border antigens, and (3) the effect of antisera on the activity of membrane-bound and solubilized maltase. In the latter study 2 parameters, binding capacity and inhibition of enzyme, were measured. Reaction of antisera with solubilized brush border antigens resulted in the removal of up to 95% of maltase from solution. This was referred to as binding capacity, because the antigen-antibody precipitate retained considerable maltase activity. Inhibition or inactivation of both solubilized and membrane-bound enzyme also occurred but was considerably lower than binding. These effects appeared to be associated with IgG immunoglobulins. Results suggest that antibodies induced by a complex array of brush border antigens from the gut of ascaris can react with specific catalytic components associated with this structure and alter activity.
ISSN:0022-3395
1937-2345
DOI:10.2307/3278687