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

Author:

Schiffmann Elliott12,Showell Henry V.12,Corcoran Barbara A.12,Ward Peter A.12,Smith Eric12,Becker Elmer L.12

Affiliation:

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

2. Department of Pathology, University of Connecticut Health Center From the , Bethesda, Maryland , and the , Farmington, Connecticut

Abstract

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.

Publisher

The American Association of Immunologists

Subject

Immunology,Immunology and Allergy

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