TY - JOUR
T1 - Purification and characterization of Microcystis aeruginosa (freshwater cyanobacterium) lectin
AU - Yamaguchi, Masato
AU - Jimbo, Mituru
AU - Sakai, Ryuichi
AU - Muramoto, Koji
AU - Kamiya, Hisao
PY - 1998/1/1
Y1 - 1998/1/1
N2 - Microcystis aeruginosa, strain M228, a laboratory culture of freshwater cyanobacterium, showed hemagglutinating activity against rabbit, horse and human ABO erthrocytes. Crossed absorption tests revealed the presence of a single type of lectin in the extract of M228 strain cells. The lectin, termed MAL, was purified in combination with the affinity chromatography on acid-treated agarose gel and the gel permeation chromatography in an electrophoretically pure form. MAL was a glycoprotein containing 7.8% neutral sugars and was composed of a single polypeptide having a molecular weight of 57 kDa. Isoelectric point was estimated to be pH 6.4. Hemagglutinating activity of the lectin was inhibited effectively by N-acetyl-d-galactosamine and by glycoproteins. d-galactose and lactose also showed moderate inhibitory activity. The destruction of the hemagglutinating activity by a 2-mercaptoethanol treatment suggests the presence of intra-chain disulfide bond(s) essential for the activity in the molecule. The sequence of the amino-terminal region of MAL was determined as Val-Lys-Ala-Ser-Lys-Val-Ser-Thr-Ser-Gln-Ala-Gly-Ser-Lys-Glu-Lys-Lys-Ala. Copyright (C) 1998 Elsevier Science Inc.
AB - Microcystis aeruginosa, strain M228, a laboratory culture of freshwater cyanobacterium, showed hemagglutinating activity against rabbit, horse and human ABO erthrocytes. Crossed absorption tests revealed the presence of a single type of lectin in the extract of M228 strain cells. The lectin, termed MAL, was purified in combination with the affinity chromatography on acid-treated agarose gel and the gel permeation chromatography in an electrophoretically pure form. MAL was a glycoprotein containing 7.8% neutral sugars and was composed of a single polypeptide having a molecular weight of 57 kDa. Isoelectric point was estimated to be pH 6.4. Hemagglutinating activity of the lectin was inhibited effectively by N-acetyl-d-galactosamine and by glycoproteins. d-galactose and lactose also showed moderate inhibitory activity. The destruction of the hemagglutinating activity by a 2-mercaptoethanol treatment suggests the presence of intra-chain disulfide bond(s) essential for the activity in the molecule. The sequence of the amino-terminal region of MAL was determined as Val-Lys-Ala-Ser-Lys-Val-Ser-Thr-Ser-Gln-Ala-Gly-Ser-Lys-Glu-Lys-Lys-Ala. Copyright (C) 1998 Elsevier Science Inc.
KW - Agglutinin
KW - Blue-green algae
KW - Cyanobacteria
KW - Hemagglutinin
KW - Lectin
KW - Microcystis aeruginosa
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U2 - 10.1016/S0305-0491(98)00033-9
DO - 10.1016/S0305-0491(98)00033-9
M3 - Article
C2 - 9734343
AN - SCOPUS:0031879697
VL - 119
SP - 593
EP - 597
JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
SN - 1096-4959
IS - 3
ER -