A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity.
A lectin from the Adriatic sponge Haliclona cratera was purified by ion-exchange and gel chromatography. The molecular mass of the lectin is approximately 29 kDa. Purified lectin is rich in hydrophobic and basic amino acids and has an isoelectric point at pH 8.6. H. cratera lectin is relatively heat- and pH-stable. It agglutinates native and trypsinized, papainized and neuraminidase-treated human A, B, O, AB and sheep erythrocytes, and the hemagglutinating activity is independent of Ca(2+), Mn(2+) and Mg(2+) ions; D-galactose and N-acetyl-D-galactosamine are found to be moderate inhibitors of the activity. H. cratera lectin displays cytotoxic effect on HeLa and FemX cells and weak mitogenic effect on human T-lymphocytes pretreated with phytohemagglutinin (PHA).
Pajic
Ivana
I
Faculty of Chemistry, University of Belgrade, Studentski trg 16, P.O. Box 158, YU-11001, Belgrade, Yugoslavia.
Kljajic
Zoran
Z
Dogovic
Nikola
N
Sladic
Dusan
D
Juranic
Zorica
Z
Gasic
Miroslav J
MJ
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001789:Blood Group Antigens; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004354:Drug Screening Assays, Antitumor; D004912:Erythrocytes / Q000187:drug effects; D006367:HeLa Cells; D006385:Hemagglutination Inhibition Tests / Q000379:methods; D006386:Hemagglutination Tests; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D008934:Mitogens / Q000494:pharmacology; D008970:Molecular Weight; D011161:Porifera / Q000737:chemistry*; D012756:Sheep; D013601:T-Lymphocytes / Q000187:drug effects; D013696:Temperature
D000596:Amino Acids; D001789:Blood Group Antigens; D037102:Lectins; D008934:Mitogens