Figure 1.

Immunoblotting of proteins purified by affinity chromatography using monoclonal antibody AHN-17. Neutrophil proteins recognized by AHN-17 were isolated by immunoaffinity chromatography, analyzed by SDS-PAGE in a 13% gel under non-reducing conditions, transferred to nitrocellulose, and immunoblotted with AHN-17 (lane A), AHN-17.1 (lane B), 15H9 (lane C), and normal mouse serum (NMS) (lane D). Proteins used as molecular weight standards were: rabbit muscle phosphorylase B, 97,000; Bovine serum albumin 66,000; ovalbumin 45,000; glyceraldehyde 3 phosphate dehydrogenase, 36,000; bovine erythrocyte carbonic anhydrase 30,000; soybean trypsin inhibitor 20,000; and bovine lactalbumin 14,000.