Purification and Characterization of a new Lectin from the Red Marine Alga Hypnea Musciformis
Authors: Nagano, C. S.; Moreno, F.B. M.B.; Bloch Jr, C.; Prates, M. V.; Calvete, J. J.; Saker-Sampaio, S.; Farias, W.R. L.; Tavares, T. D.; Nascimento, K. S.; Grangeiro, T. B.; Cavada, B. S.; Sampaio, A. H.
A lectin from the red marine alga Hypnea musciformis (HML) was purified by extraction with 20 mM PBS, precipitation with 70% saturated ammonium sulphate, ion-exchange DEAE-Cellulose chromatography and RP-HPLC. The 9.3 kDa polypeptide agglutinates erythrocytes from various sources and shows oligomerization tendencies under certain MALDI-TOF / MS conditions. Preliminary N-terminal sequencing and biological assays strongly suggest that the HML may belong to a new class of algae lectins.
Laboratorio de Bioquimica Marinha - BioMol-Lab, Depto de Engenharia de Pesca, Universidade Federal do Ceara, Caixa postal 6033, CEP 60451-970
Publication date: April 1, 2002
More about this publication?
Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.