חיפוש מתקדם
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
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.
פותח על ידי קלירמאש פתרונות בע"מ -
הספר "אוצר וולקני"
אודות
תנאי שימוש
Isolation of a mannose-specific lectin from Escherichia coli and its role in the adherence of the bacteria to epithelial cells
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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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