A 56 kDa binding protein for Escherichia coli heat-stable enterotoxin isolated from the cytoskeleton of rat intestinal membrane does not possess guanylate cyclase activity.
Publication/Presentation Date
10-10-1993
Abstract
Proteins binding Escherichia coli heat-stable enterotoxin were isolated from the cytoskeleton of intestinal membranes using an affinity matrix of biotinylated ST immobilized on monomeric avidin-agarose. ST binding proteins were purified 343-fold using this affinity technique, with 7% of the initial binding activity recovered in these preparations. ST binding proteins isolated by affinity chromatography possessed a native and subunit molecular mass of 56 kDa. These preparations exhibited both high- and low-affinity binding sites for ST. Guanylate cyclase in extracts of the intestinal membrane cytoskeleton was completely recovered in fractions which did not associate with the affinity matrix. In addition, ST binding proteins isolated by affinity chromatography were devoid of guanylate cyclase activity. These data, taken together with those obtained previously with crude and partially purified receptors, suggest that ST binds to different proteins in intestinal membranes, some of which do not possess guanylate cyclase activity.
Volume
1152
Issue
1
First Page
1
Last Page
8
ISSN
0006-3002
Published In/Presented At
Hakki, S., Robertson, D. C., & Waldman, S. A. (1993). A 56 kDa binding protein for Escherichia coli heat-stable enterotoxin isolated from the cytoskeleton of rat intestinal membrane does not possess guanylate cyclase activity. Biochimica et biophysica acta, 1152(1), 1–8. https://doi.org/10.1016/0005-2736(93)90224-n
Disciplines
Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods
PubMedID
8104484
Department(s)
Administration and Leadership
Document Type
Article