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The Journal of Immunology, 1975, 114, 1831 -1837
Copyright © 1975 by The American Association of Immunologists, Inc.

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The Isolation and Partial Characterization of Neutrophil Chemotactic Factors from Escherichia Coli

Elliott Schiffmann1, Henry V. Showell2,3,, Barbara A. Corcoran1, Peter A. Ward2,4,, Eric Smith5 and Elmer L. Becker2,3,

From the Laboratory of Developmental Biology and Anomalies, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland, and the Department of Pathology, University of Connecticut Health Center, Farmington, Connecticut

Abstract

Heat-stable, chemotactically active peptides have been obtained from Escherichia coli culture filtrates. They range in size between 150 and 1500 daltons and are anionic at neutral pH. Free carboxyl groups but not free amino groups appear to be required for activity. The N-terminal group may be blocked. There do not appear to be internal aromatic or basic residues in the chemotactically active fractions. A highly purified, not completely characterized, fraction was found to contain aspartic acid, serine, glutamic acid, alanine, and glycine.

Footnotes

1 From the Laboratory of Developmental Biology and Anomalies, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 20014.

2 From the Department of Pathology, University of Connecticut Health Center, Farmington, Connecticut 06032

3 This work was supported by United States Public Health Service Research Grant A109648.

4 This work was supported by United States Public Health Service Research Grant AT0109651.

5 This work was supported by United States Public Health Service Training Grant 5T01A100438.




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