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Similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6936237
The eosinophil granule contains a series of basic proteins, including eosinophil-derived neurotoxin (EDN) and eosinophil cationic protein (ECP). EDN and ECP were isolated from eosinophil granules by heparin-Sepharose chromatography. Radioimmunoassay of fractions from heparin-Sepharose showed one peak of EDN activity and two peaks of ECP activity (termed ECP-1 and ECP-2). EDN, ECP-1, and ECP-2 each exhibited heterogeneity in charge and molecular weight when analyzed by two-dimensional electrophoresis. Digestion of EDN and both ECP's with endoglycosidase-F decreased their molecular weights indicating that their heterogeneity is due in part to n-linked oligosaccharides. Amino acid sequence analyses showed that ECP-1 and ECP-2 were identical from residues 1 through 59 and that EDN and ECP sequences were highly homologous (37 of 55 residues identical). Both EDN and ECP NH/sub 2/-terminal sequences showed significant homology to RNase, especially in regions of the RNase molecule involved in ligand binding. EDN, ECP-1 and ECP-2 had neurotoxic activity, causing the Gordon phenomenon at doses down 0.15 microgram; the proteins were comparable in their activities. These results indicate that EDN and ECP are related proteins and suggest that they derived from genes associated with the RNase family.
Research Organization:
Mayo Clinic and Foundation, Rochester, MN
OSTI ID:
6936237
Report Number(s):
CONF-8604222-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 45:4
Country of Publication:
United States
Language:
English