A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity
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2002
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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.
Ključne reči:
sponge / Haliclona cratera / lectin / purification / isolation / stability / cytotoxicityIzvor:
Comparative Biochemistry and Physiology. C: Toxicology and Pharmacology, 2002, 132, 2, 213-221Izdavač:
- 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
Institucija/grupa
IHTMTY - JOUR AU - Pajic, I AU - Kljajic, Z AU - Dogović, Nikola AU - Sladić, Dušan AU - Juranić, Zorica AU - Gašić, Miroslav J. PY - 2002 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/2837 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 Dogović, Nikola and Sladić, Dušan and Juranić, Zorica and Gašić, Miroslav J.", 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., Dogović, N., Sladić, D., Juranić, Z.,& Gašić, M. J.. (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, Dogović N, Sladić D, Juranić Z, Gašić MJ. 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, Dogović, Nikola, Sladić, Dušan, Juranić, Zorica, Gašić, Miroslav J., "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 . .