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Isolation of a mannose-specific lectin from Escherichia coli and its role in the adherence of the bacteria to epithelial cells
Year:
1978
Authors :
Eshdat, Yuval
;
.
Volume :
85
Co-Authors:
Eshdat, Y., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Ofek, I., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Yashouv-Gan, Y., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Sharon, N., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Mirelman, D., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Facilitators :
From page:
1551
To page:
1559
(
Total pages:
9
)
Abstract:
A high molecular weight protein aggregate, which agglutinates yeast cells, human epithelial cells and mouse lymphocytes, was isolated from extracts of Escherichia coli by differential centrifugation and gel filtration. The agglutination is specifically inhibited by d-mannose and its derivatives, the best inhibitor being p-nitrophenyl α-d-mannoside. Sodium dodecyl sulfate gel electrophoresis showed that the lectin consists of protein subunits with identical Mr of ∼36500. The amino acid composition of the purified lectin is different from that reported for the type I pili protein, the K99 antigen and the major outer membrane protein Ia of E. coli. The protein appears to be located on the bacterial surface, and is probably involved in the mannose-specific adherence of E. coli to eukaryotic cells. © 1978.
Note:
Related Files :
Agglutination
Amino Acids
animal experiment
Epithelium
Escherichia coli
Humans
lectins
Mannosides
Skin Physiology
Show More
Related Content
More details
DOI :
10.1016/0006-291X(78)91179-8
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
18863
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:24
Scientific Publication
Isolation of a mannose-specific lectin from Escherichia coli and its role in the adherence of the bacteria to epithelial cells
85
Eshdat, Y., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Ofek, I., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Yashouv-Gan, Y., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Sharon, N., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Mirelman, D., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Isolation of a mannose-specific lectin from Escherichia coli and its role in the adherence of the bacteria to epithelial cells
A high molecular weight protein aggregate, which agglutinates yeast cells, human epithelial cells and mouse lymphocytes, was isolated from extracts of Escherichia coli by differential centrifugation and gel filtration. The agglutination is specifically inhibited by d-mannose and its derivatives, the best inhibitor being p-nitrophenyl α-d-mannoside. Sodium dodecyl sulfate gel electrophoresis showed that the lectin consists of protein subunits with identical Mr of ∼36500. The amino acid composition of the purified lectin is different from that reported for the type I pili protein, the K99 antigen and the major outer membrane protein Ia of E. coli. The protein appears to be located on the bacterial surface, and is probably involved in the mannose-specific adherence of E. coli to eukaryotic cells. © 1978.
Scientific Publication
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