Faculty of Chemistry Repository - Cherry
University of Belgrade - Faculty of Chemistry
    • English
    • Српски
    • Српски (Serbia)
  • English 
    • English
    • Serbian (Cyrilic)
    • Serbian (Latin)
  • Login
View Item 
  •   Faculty of Chemistry Repository - Cherry
  • Hemijski fakultet
  • Publikacije
  • View Item
  •   Faculty of Chemistry Repository - Cherry
  • Hemijski fakultet
  • Publikacije
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity

Authorized Users Only
2002
Authors
Pajic, I
Kljajic, Z
Dogovic, N
Sladić, Dušan
Juranic, Z
Gasic, MJ
Article (Published version)
Metadata
Show full item record
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 / cytotoxicity
Source:
Comparative Biochemistry and Physiology. C: Toxicology and Pharmacology, 2002, 132, 2, 213-221
Publisher:
  • 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
[ Google Scholar ]
47
42
URI
http://cherry.chem.bg.ac.rs/handle/123456789/501
Collections
  • Publikacije
Institution
Hemijski fakultet
TY  - JOUR
AU  - Pajic, I
AU  - Kljajic, Z
AU  - Dogovic, N
AU  - Sladić, Dušan
AU  - Juranic, Z
AU  - Gasic, MJ
PY  - 2002
UR  - http://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 Juranic, Z and Gasic, MJ",
year = "2002",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/501",
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, Juranic Z, Gasic M. A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity. Comparative Biochemistry and Physiology. C: Toxicology and Pharmacology. 2002;132(2):213-221
Pajic, I., Kljajic, Z., Dogovic, N., Sladić, D., Juranic, Z.,& Gasic, M. (2002). A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity.
Comparative Biochemistry and Physiology. C: Toxicology and PharmacologyElsevier 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 Dušan, Juranic Z, Gasic MJ, "A novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activity" 132, no. 2 (2002):213-221,
https://doi.org/10.1016/S1532-0456(02)00068-6 .

DSpace software copyright © 2002-2015  DuraSpace
About CHERRY - CHEmistry RepositoRY | Send Feedback

OpenAIRERCUB
 

 

All of DSpaceInstitutionsAuthorsTitlesSubjectsThis institutionAuthorsTitlesSubjects

Statistics

View Usage Statistics

DSpace software copyright © 2002-2015  DuraSpace
About CHERRY - CHEmistry RepositoRY | Send Feedback

OpenAIRERCUB