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Erratum to “Purification and characterization of antimicrobial and vasorelaxant peptides from skin extracts and skin secretions of the North American pig frog Rana grylio”
Regulatory Peptides 91 (2000) 107–108 www.elsevier.com / locate / regpep
Erratum
Erratum to ‘‘Purification and characterization of antimicrobial and vasorelaxant peptides from skin extracts and skin secretions of the North American pig frog Rana grylio’’ [Regul. Pept. 90 (2000) 53–60] q Joseph B. Kim a , Thomas Halverson a , Yousef J. Basir a , Joseph Dulka b , Floyd C. Knoop c , d a, Peter W. Abel , J. Michael Conlon * a
Regulatory Peptide Center, Department of Biomedical Sciences, Creighton University Medical School, Omaha, NE 68178, USA b Department of Biology, Creighton University, Omaha, NE 68178, USA c Department of Medical Microbiology and Immunology, Creighton University Medical School, Omaha, NE 68178, USA d Department of Pharmacology, Creighton University Medical School, Omaha, NE 68178, USA Received 30 June 2000
The Publisher regrets that Figs. 5 and 6 (pp. 58 and 59) in the above paper were incorrectly labelled. The correct figures with appropriate legends are now printed overleaf.
q
PII of original article: S 0 1 6 7 - 0 1 1 5 ( 0 0 ) 0 0 1 0 7 - 5 *Corresponding author. Tel.: 1 1-402-280-1733; fax: 1 1-402-280-2690. E-mail address: [email protected] (J.M. Conlon). 0167-0115 / 00 / $ – see front matter 2000 Elsevier Science B.V. All rights reserved. PII: S0167-0115( 00 )00159-2
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Fig. 6. Antimicrobial peptides isolated from skin extracts and skin secretions of Rana grylio grouped into four families on the basis of structural similarity. The families are named after the first peptide in that family to have been described. Ranalexin, ranatuerin-1, ranatuerin-2, and ranatuerins 5–9 are from R. catesbeiana, ranalexin-1Ca and -1Cb, ranatuerin-1C, ranatuerin-2Ca and -2Cb, and temporins 1Ca-1Ce are from R. clamitans, ranatuerin-2B is from R. berlandieri, ranatuerin-2P is from R. pipiens and temporin A is from R. temporaria. In order to maximize structural similarity, deletions denoted by (*) have been introduced into some sequences. (-) denotes residue identity. Fig. 5. Mean concentration-response curves for temporin-induced relaxation of rat thoracic aorta precontracted with KCl. Panel A. Relaxation produced by temporin-1Gb. Panel B. Relaxation produced by temporin1Gd. Note that both peptides caused only a partial relaxation of KClinduced tone. Each curve is the mean of four concentration-response curves, each obtained in a tissue from a different animal.
Erratum
Erratum to ‘‘Purification and characterization of antimicrobial and vasorelaxant peptides from skin extracts and skin secretions of the North American pig frog Rana grylio’’ [Regul. Pept. 90 (2000) 53–60] q Joseph B. Kim a , Thomas Halverson a , Yousef J. Basir a , Joseph Dulka b , Floyd C. Knoop c , d a, Peter W. Abel , J. Michael Conlon * a
Regulatory Peptide Center, Department of Biomedical Sciences, Creighton University Medical School, Omaha, NE 68178, USA b Department of Biology, Creighton University, Omaha, NE 68178, USA c Department of Medical Microbiology and Immunology, Creighton University Medical School, Omaha, NE 68178, USA d Department of Pharmacology, Creighton University Medical School, Omaha, NE 68178, USA Received 30 June 2000
The Publisher regrets that Figs. 5 and 6 (pp. 58 and 59) in the above paper were incorrectly labelled. The correct figures with appropriate legends are now printed overleaf.
q
PII of original article: S 0 1 6 7 - 0 1 1 5 ( 0 0 ) 0 0 1 0 7 - 5 *Corresponding author. Tel.: 1 1-402-280-1733; fax: 1 1-402-280-2690. E-mail address: [email protected] (J.M. Conlon). 0167-0115 / 00 / $ – see front matter 2000 Elsevier Science B.V. All rights reserved. PII: S0167-0115( 00 )00159-2
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Fig. 6. Antimicrobial peptides isolated from skin extracts and skin secretions of Rana grylio grouped into four families on the basis of structural similarity. The families are named after the first peptide in that family to have been described. Ranalexin, ranatuerin-1, ranatuerin-2, and ranatuerins 5–9 are from R. catesbeiana, ranalexin-1Ca and -1Cb, ranatuerin-1C, ranatuerin-2Ca and -2Cb, and temporins 1Ca-1Ce are from R. clamitans, ranatuerin-2B is from R. berlandieri, ranatuerin-2P is from R. pipiens and temporin A is from R. temporaria. In order to maximize structural similarity, deletions denoted by (*) have been introduced into some sequences. (-) denotes residue identity. Fig. 5. Mean concentration-response curves for temporin-induced relaxation of rat thoracic aorta precontracted with KCl. Panel A. Relaxation produced by temporin-1Gb. Panel B. Relaxation produced by temporin1Gd. Note that both peptides caused only a partial relaxation of KClinduced tone. Each curve is the mean of four concentration-response curves, each obtained in a tissue from a different animal.