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dc.creatorPajic, I
dc.creatorKljajic, Z
dc.creatorDogović, Nikola
dc.creatorSladić, Dušan
dc.creatorJuranić, Zorica
dc.creatorGašić, Miroslav J.
dc.date.accessioned2019-05-02T13:47:47Z
dc.date.available2019-05-02T13:47:47Z
dc.date.issued2002
dc.identifier.issn1532-0456
dc.identifier.urihttps://cer.ihtm.bg.ac.rs/handle/123456789/2837
dc.description.abstractA 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.en
dc.publisherElsevier Science Inc, New York
dc.rightsrestrictedAccess
dc.sourceComparative Biochemistry and Physiology. C: Toxicology and Pharmacology
dc.subjectspongeen
dc.subjectHaliclona crateraen
dc.subjectlectinen
dc.subjectpurificationen
dc.subjectisolationen
dc.subjectstabilityen
dc.subjectcytotoxicityen
dc.titleA novel lectin from the sponge Haliclona cratera: isolation, characterization and biological activityen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractЈураниц, З; Гасиц, МЈ; Пајиц, И; Кљајиц, З; Договић, Никола; Сладић, Душан;
dc.citation.volume132
dc.citation.issue2
dc.citation.spage213
dc.citation.epage221
dc.citation.other132(2): 213-221
dc.citation.rankM22
dc.identifier.pmid12106898
dc.identifier.doi10.1016/S1532-0456(02)00068-6
dc.identifier.scopus2-s2.0-0035996841
dc.identifier.wos000177257300010
dc.type.versionpublishedVersionen


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