期刊
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
卷 125, 期 2, 页码 169-177出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/S0305-0491(99)00164-9
关键词
agglutinins; blue-green algae; cyanobacteria; carbohydrate-binding specificity; isolation; lectin; Eucheuma; Myxococcus xanthus; Oscillatoria agardhii; N-terminal sequence
In the survey of 14 species of laboratory-cultured cyanobacteria for hemagglutinins, we newly detected the activity in two species, Oscillatoria agardhii; strain NIES-204, and Phormidium foveolarum, Strain NIES-503. From the extract of O. agardhii, which showed the highest activity with trypsin-treated erythrocytes of rabbit, a lectin was purified to homogeneity by the combination of precipitation with (NH4)(2)SO4, pel filtration, hydrophobic chromatography and reverse phase chromatography. The purified lectin, designated OAA, was a monomeric protein with an apparent molecular weight of 13 000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 16 000 on gel filtration. The amino acid composition was rich in glycine and acidic amino acids. The hemagglutination activity was inhibited by glycoproteins such as yeast mannan, but not by any of the monosaccharides tested. The activity was stable over a wide range of pH (4-11) and at a high temperature of 80 degrees C, and independent on the presence of divalent cations. The features of OAA resembled those of many of lectins from marine macroalgae. The sequence of amino-terminal residues of OAA was determined as ALYNVENQWGGSSAPWNEGG; which was highly homologous to those of lectins from macroalgae of the genus Eucheuma and that of a myxobacterium Myxococcus xanthus hemagglutinin. (C) 2000 Elsevier Science Inc. All rights reserved.
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