A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity
Abstract
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 Ca2+, Mn2+ and Mg2+ 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). (C) 2002 Elsevier Science Inc. All rights reserved.
Keywords:
sponge / Haliclona cratera / lectin / purification / isolation / stability / cytotoxicitySource:
Comparative Biochemistry and Physiology. C: Toxicology and Pharmacology, 2002, 132, 2, 213-221Publisher:
- Elsevier Science Inc, New York
DOI: 10.1016/S1532-0456(02)00068-6
ISSN: 1532-0456
PubMed: 12106898
WoS: 000177257300010
Scopus: 2-s2.0-0035996841
Collections
Institution/Community
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Pajic, I AU - Kljajic, Z AU - Dogovic, N AU - Sladić, Dušan AU - Juranić, Z. AU - Gasic, MJ PY - 2002 UR - https://cherry.chem.bg.ac.rs/handle/123456789/501 AB - 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 Ca2+, Mn2+ and Mg2+ 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). (C) 2002 Elsevier Science Inc. All rights reserved. PB - Elsevier Science Inc, New York T2 - Comparative Biochemistry and Physiology. C: Toxicology and Pharmacology T1 - A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity VL - 132 IS - 2 SP - 213 EP - 221 DO - 10.1016/S1532-0456(02)00068-6 ER -
@article{ author = "Pajic, I and Kljajic, Z and Dogovic, N and Sladić, Dušan and Juranić, Z. and Gasic, MJ", year = "2002", abstract = "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 Ca2+, Mn2+ and Mg2+ 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). (C) 2002 Elsevier Science Inc. All rights reserved.", publisher = "Elsevier Science Inc, New York", journal = "Comparative Biochemistry and Physiology. C: Toxicology and Pharmacology", title = "A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity", volume = "132", number = "2", pages = "213-221", doi = "10.1016/S1532-0456(02)00068-6" }
Pajic, I., Kljajic, Z., Dogovic, N., Sladić, D., Juranić, Z.,& Gasic, M.. (2002). A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity. in Comparative Biochemistry and Physiology. C: Toxicology and Pharmacology Elsevier Science Inc, New York., 132(2), 213-221. https://doi.org/10.1016/S1532-0456(02)00068-6
Pajic I, Kljajic Z, Dogovic N, Sladić D, Juranić Z, Gasic M. A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity. in Comparative Biochemistry and Physiology. C: Toxicology and Pharmacology. 2002;132(2):213-221. doi:10.1016/S1532-0456(02)00068-6 .
Pajic, I, Kljajic, Z, Dogovic, N, Sladić, Dušan, Juranić, Z., Gasic, MJ, "A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity" in Comparative Biochemistry and Physiology. C: Toxicology and Pharmacology, 132, no. 2 (2002):213-221, https://doi.org/10.1016/S1532-0456(02)00068-6 . .