2026-06-28T15:20:10Zhttps://docta.ucm.es/rest/oai/request
oai:docta.ucm.es:20.500.14352/1026282025-03-18T15:21:16Zcom_20.500.14352_14col_20.500.14352_15
Docta Complutense author Martínez Ruiz, Antonio author Martínez Del Pozo, Álvaro author Lacadena García-Gallo, Francisco Javier author Mancheño Gómez, José Miguel author Oñaderra Sánchez, Mercedes author Gavilanes Franco, José Gregorio 2024-04-03T14:37:29Z 2024-04-03T14:37:29Z 1997-06 Martı́nez-Ruiz, A., Martı́nez del Pozo, A., Lacadena, J., Mancheño, J. M., Oñaderra, M., & Gavilanes, J. G. (1997). Characterization of a natural larger form of the antifungal protein (AFP) from Aspergillus giganteus. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1340(1), 81–87. doi:10.1016/s0167-4838(97)00038-1 0167-4838 10.1016/s0167-4838(97)00038-1 https://hdl.handle.net/20.500.14352/102628 Two major proteins, a-sarcin and an antifungal polypeptide AFP , are secreted by the mould Ž . Aspergillus giganteus MDH 18894 when it is cultured for 70–80 h. A third major protein is also found in the extracellular medium at 48–60 h, but it disappears as the culture proceeds. This protein has been isolated and characterized in terms of apparent molecular mass, electrophoretic and chromatographic behaviour, NH -terminal primary structure, amino acid content, spectroscopical 2 features, reactivity against anti-AFP antibodies, and antifungal activity. Based on the obtained results it would be an extracellular inactive precursor form of AFP, designated as the large form of AFP lf-AFP . Its amino acid composition is Ž . identical to that of AFP but containing six extra residues. NH -terminal sequence analysis of the first eight amino acid 2 residues of this polypeptide revealed that the extra residues can be perfectly accommodated within the DNA-deduced sequence of the precursor form of AFP. Its alignment with precursor sequences of different proteins, secreted by a variety of Aspergillus spp., reveals the existence of a common tetrapeptide at the carboxy-terminal end of their leader peptides. This sequence would be IlerLeu-Xaa-Yaa-Arg, being mostly Xaa and Yaa an acid residue Asp Ž . rGlu and alanine, respectively. The presence of lf-AFP as an extracellular protein would be in perfect agreement with the existence of this tetrapeptide motif, that can be involved in the protein secretion mechanisms of filamentous fungi. eng Characterization of a natural larger form of the antifungal protein (AFP) from Aspergillus giganteus journal article 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