Heterogeneity of intestinal receptors for Escherichia coli heat-stable enterotoxin.
Publication/Presentation Date
6-1-1990
Abstract
The structure of rat intestinal cell receptors for Escherichia coli heat-stable enterotoxin (ST) was investigated by affinity cross-linking to 125I-ST and analysis by denaturing gel electrophoresis. Cross-linking of labeled toxin to intestinal membranes and analysis by nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed five specifically labeled proteins with molecular masses of 160, 136, 78, 71, and 56 (kilodaltons) kDa. Exhaustive reduction of these samples resulted in a similar pattern of labeling. Affinity-labeled proteins were further analyzed by nonreducing SDS-PAGE, reduction of the resulting separated proteins, and further separation by SDS-PAGE in the presence of beta-mercaptoethanol. Thus, the 160-kDa band on nonreducing gels consisted of two different receptors: a 160-kDa polypeptide not further reducible and one composed of at least two subunits, one of which was the 78-kDa subunit. Similarly, the 136-kDa band on nonreducing gels consisted of a 136-kDa polypeptide not further reducible and one composed of at least two subunits, one of which was the 71-kDa subunit. The 78-, 71-, and 56-kDa subunits were not further reducible. These data suggest heterogeneity of the ST receptor subunit structure and organization in rat intestinal epithelia.
Volume
58
Issue
6
First Page
1817
Last Page
1820
ISSN
0019-9567
Published In/Presented At
Ivens, K., Gazzano, H., O'Hanley, P., & Waldman, S. A. (1990). Heterogeneity of intestinal receptors for Escherichia coli heat-stable enterotoxin. Infection and immunity, 58(6), 1817–1820. https://doi.org/10.1128/iai.58.6.1817-1820.1990
Disciplines
Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods
PubMedID
2160433
Department(s)
Administration and Leadership
Document Type
Article