©95 by The American Society for Biochemistry and Molecular Biology, Inc.
Additions and Corrections to Eosinophil cationic protein and eosinophil-derived neurotoxin. Evolution of novel function in a primate ribonuclease gene family.

Helene F. Rosenberg Kimberly D. Dyer


Vol. 270, p. 21539

Page 21542, Fig. 4: The reproduction of panels B-D was inadequate. An improved version is shown below with corrected figure legend.


Figure 4: A, amino acid sequence comparisons of human EDN, marmoset EDN (mEDN), and human ECP. Numbered boxes enclose the conserved catalytic residues (His, Lys, His); boxes with bold outline enclose the conserved cyste ines. Open rectangles denote residues shared by EDN and mEDN but not by ECP and residues shared by ECP and mEDN but not by EDN; open squares enclose those residues unique to mEDN. The percentage similarity of mEDN to both EDN and ECP, as well as the calculated isoelectric point of each sequence are listed in the final columns. B, Western blot containing total cell extracts of IPTG-induced bacterial transfectants probed with M2 mAb. Lane 1, recombinant ECP; lane 2, recombinant EDN; lane 3, recombinant mEDN. C and D are identical blots probed with polyclonal anti-EDN and anti-ECP antisera, respectively. E, percentage of CFUs of S. aureus surviving after a 4-h incubation at 37 °C with recombinant EDN (open circles), recombinant mEDN (filled circles), and recombinant ECP (open squares). Each point represents the average of triplicate samples; error bars as indicated.




©95 by The American Society for Biochemistry and Molecular Biology, Inc.