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First published online August 8, 2008
Journal of Experimental Biology 211, 2707-2711 (2008)
Published by The Company of Biologists 2008
doi: 10.1242/jeb.019315
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Novel surfactant proteins are involved in the structure and stability of foam nests from the frog Leptodactylus vastus

Denise Cavalcante Hissa1, Ilka Maria Vasconcelos2, Ana Fontenele Urano Carvalho1, Vanessa Lúcia Rodrigues Nogueira1, Paulo Cascon1, André Saraiva Leão Antunes1, Gorete Ribeiro de Macedo3 and Vânia Maria Maciel Melo1,*

1 Departamento de Biologia, Universidade Federal do Ceará, Av. Humberto Monte 2775 Campus Pici, Bloco 909, Fortaleza, Brazil, 60455-000
2 Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Campus Pici, Fortaleza, Brazil
3 Departamento de Engenharia Química, Universidade Federal do Rio Grande do Norte, Natal, Brazil


Figure 1
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  		Fig. 1. (A) Foam nests of Leptodactylus vastus (B).

 

Figure 2
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  		Fig. 2. Denaturing Tricine-SDS-PAGE of the foam fluid and fractions obtained during isolation of the surfactant 20 kDa protein. Lane 1, molecular mass standards; lane 2, foam fluid (20 µg); lanes 3 and 4, non-retained and retained fractions, respectively, in CM-Sepharose (20 µg). Molecular mass markers were phosphorylase b (97.0 kDa), bovine serum albumin (67.0 kDa), egg white albumin (45.0 kDa), carbonic anhydrase (29.0 kDa), soybean trypsin inhibitor (20.1 kDa) and {alpha}-lactalbumin (14.2 kDa).

 

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