Open Access

ARTICLE

A first attempt to elucidate the amino acid sequence of some lichen lectins

Sacristán M, AM Millanes, B Fontaniella, ME Legaz, C Vicente

Department of Plant Physiology, The Lichen Team. Faculty of Biology, Complutense University. JoséAntonio Novais s/n, 28040 Madrid, Spain
Address Correspondence to: Prof. Dr. Carlos Vicente. Department of Plant Physiology, Faculty of Biology, José Antonio Novais st., s/n. Complutense University, 28040 Madrid, Spain. Phone number: 34-1-3944565, Fax number: 34-1-3945034. e-mail: cvicente@bio.ucm.es

Phyton-International Journal of Experimental Botany 2008, 77(all), 253-262. https://doi.org/10.32604/phyton.2008.77.253

Abstract

Secreted arginases from Evernia prunastri and Xanthoria parietina thalli, 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.

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