2026-06-01T07:24:29Zhttps://docta.ucm.es/rest/oai/requestoai:docta.ucm.es:20.500.14352/1082912025-03-18T15:01:46Zcom_20.500.14352_14col_20.500.14352_15
A first attempt to elucidate the amino acid sequence of some lichen lectins
Sacristán, M.
Millanes, A. M.
Fontaniella López, Blanca
Legaz González, María Estrella
Vicente Córdoba, Carlos
582.29
581.1
Arginases
Evernia prunastri
Lectins
Structure analysis
Xanthoria parietina
Botánica (Biología)
Fisiología vegetal (Biología)
2417 Biología Vegetal (Botánica)
2417.19 Fisiología Vegetal
Secreted arginases from Evernia prunastri and Xanthoria parietina thalii, exhibiting lectin activity, have been purified to homogeneity. Analyses of both amino acid and glycoside composition are reported. Purified proteins have been subjected to tryptic digestion and some amino acid sequences have been analyzed. An undecapeptide from Evernia arginase, which shows some degree of homology with the domain to which Mn2+ binds, a heptapeptide and an undecapeptide from Xanthoria arginase have been analyzed, and homologies with some arginases from other fungi and plants have been found.
Ministerio de Ciencia y Tecnología (España)
Depto. de Biodiversidad, Ecología y Evolución
Fac. de Ciencias Biológicas
TRUE
pub
2024-09-20T14:34:45Z
2024-09-20T14:34:45Z
2008
journal article
VoR
https://hdl.handle.net/20.500.14352/108291
0031-9457
1851-5657
eng
info:eu-repo/grantAgreement/MCYT//BFI2003-06234
Sacristán, et al. «A first attempt to elucidate the amino acid sequence of some lichen lectins». Phyton, vol. 77, 2008, pp. 253-62.
restricted access
application/pdf
Fundación Romulo Raggio