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Purification and characterization of a new lectin from the red marine alga Hypnea musciformis.

Nagano, C S; Moreno, F B M B; Bloch, 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.

Protein Pept Lett ; 9(2): 159-66, 2002 Apr.

Article in English | MEDLINE | ID: mdl-12141914

ABSTRACT

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.

Subject(s)

Lectins/chemistry , Lectins/isolation & purification , Rhodophyta/metabolism , Animals , Chromatography, High Pressure Liquid , Chromatography, Ion Exchange , Dimerization , Humans , Protein Structure, Tertiary , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

ABSTRACT

Subject(s)

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