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Cell Mol Life Sci ; 57(2): 343-50, 2000 Feb.
Article in English | MEDLINE | ID: mdl-10766029

ABSTRACT

The primary structure of a lectin isolated from the red alga Bryothamnion triquetrum was established by combination of Edman degradation of sets of overlapping peptides and mass spectrometry. It contains 91 amino acids and two disulphide bonds. The primary structure of the B. triquetrum lectin does not show amino acid sequence similarity with known plant and animal lectin structures. Hence, this protein may be the paradigm of a novel lectin family.


Subject(s)
Algal Proteins , Lectins/chemistry , Lectins/isolation & purification , Rhodophyta/chemistry , Amino Acid Sequence , Chromatography, High Pressure Liquid , Cysteine/analysis , Disulfides/analysis , Galactosamine/analysis , Glucosamine/analysis , Lectins/classification , Lectins/metabolism , Molecular Sequence Data , Molecular Weight , Peptide Fragments/chemistry , Peptide Fragments/isolation & purification , Peptide Fragments/metabolism , Protein Isoforms/chemistry , Protein Isoforms/isolation & purification , Protein Isoforms/metabolism , Sequence Analysis, Protein , Sequence Homology, Amino Acid , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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