Autor: |
Nagano CS; Laboratório de Bioquímica Marinha - BioMol-Lab, Depto de Engenharia de Pesca, Universidade Federal do Ceará, Caixa Postal 6033, CEP 60451-970, Brasil., Moreno FB, Bloch C Jr, Prates MV, Calvete JJ, Saker-Sampaio S, Farias WR, Tavares TD, Nascimento KS, Grangeiro TB, Cavada BS, Sampaio AH |
Jazyk: |
angličtina |
Zdroj: |
Protein and peptide letters [Protein Pept Lett] 2002 Apr; Vol. 9 (2), pp. 159-66. |
DOI: |
10.2174/0929866023408931 |
Abstrakt: |
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. |
Databáze: |
MEDLINE |
Externí odkaz: |
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