0000000000350156

AUTHOR

Zoran Kljajić

showing 4 related works from this author

A novel galactose- and arabinose-specific lectin from the sponge Pellina semitubulosa: isolation, characterization and immunobiological properties.

1992

A new lectin from the sponge Pellina semitubulosa is derived which was extracted and purified to homogeneity. The purified lectin is probably a hexamer of polypeptide chains (each M(r) 34,000) which are covalently linked via disulfide linkages; the isoelectric point is 6.1. The lectin displays the following specificities: D-galactose (50% inhibition of hemagglutination at 0.2 mM) = L-arabinose (0.2 mM) greater than D-fucose (1.5 mM) greater than D-glucose (3.0 mM). It precipitates human erythrocytes (A1, A2, A1B, B, and O) with a titer between 2(8) and 2(11) and erythrocytes from sheep and rabbits with a titer between 2(5) and 2(10). The Pellina lectin displays a strong mitogenic effect on …

Interleukin 2HemagglutinationChemical PhenomenaLymphocyte ActivationBiochemistrySubstrate Specificitychemistry.chemical_compoundLectinsmedicineAnimalsLymphocytesAmino AcidsbiologyChemistry PhysicalMacrophagesInterleukinLectinGalactoseGeneral MedicineHemagglutination TestsMolecular biologyArabinosePoriferaTiterIsoelectric pointchemistryBiochemistryConcanavalin AGalactosebiology.proteinInterleukin-2medicine.drugInterleukin-1Biochimie
researchProduct

A D-mannose-specific lectin from Gerardia savaglia that inhibits nucleocytoplasmic transport of mRNA.

1987

A new lectin has been isolated from the coral Gerardia savaglia by affinity chromatography, using locust gum as an absorbent, and D-mannose as eluant. Final purification was achieved by Bio-Gel P300 gel filtration. The agglutinin is a protein composed of two polypeptide chains with a Mr of 14800; the two subunits are not linked by disulfide bond(s). The isoelectric point is 4.8, the amino acid composition is rich in the acidic amino acids aspartic acid and glutamic acid. The absorption maximum for the protein was at 276 nm; with a molar absorption coefficient of 1.27 X 10(5) M-1 cm-1. The lectin precipitated erythrocytes from humans (A, B and O), sheep, rabbit and carp with a titer between …

ElectrophoresisPore complexCytoplasmChemical PhenomenaMacromolecular SubstancesMannoseMitosisBiochemistryChromatography Affinity03 medical and health scienceschemistry.chemical_compoundCnidariaMiceAgglutininAffinity chromatographyLectinsAnimalsLymphocytesRNA MessengerAmino Acids030304 developmental biologyGlycoproteinsCell Nucleus0303 health sciencesbiologyChemistry Physical030302 biochemistry & molecular biologyLectinNuclear ProteinsHemagglutination Inhibition TestsNuclear matrixMolecular biologyMolecular WeightIsoelectric pointBiochemistrychemistryConcanavalin Abiology.proteinMannoseEuropean journal of biochemistry
researchProduct

The Galactose-Specific Lectin from the Sponge Chondrilla Nucula Displays Anti-Human Immunodeficiency Virus Activity in vitro via Stimulation of the (…

1990

A new lectin has been isolated from the sponge Chondrilla nucula. The purified CN lectin is a protein composed of four polypeptide chains with a molecular weight (MW) of 15600. The isoelectric point is 4.5 and the amino acid composition is rich in aspartic and glutamic acid. The lectin precipitates erythrocytes from humans (A, B, O) with a titre between 25 and 210. The CN lectin is d-galactose-specific and displays a moderate mitogenic effect on spleen lymphocytes from mice and on CD4-positive human H9 cells. An interesting feature of this lectin is its ability to stimulate the (2′-5′)oligoriboadenylate [(2′-5′)A] metabolic pathway in non-infected and human immunodeficiency virus (HIV-1)-i…

0301 basic medicinebiology2'-5'-Oligoadenylate030106 microbiologyLectinGeneral MedicineGlutamic acidbiology.organism_classification01 natural sciencesIn vitro0104 chemical sciences010404 medicinal & biomolecular chemistry03 medical and health sciencesIsoelectric pointBiochemistryConcanavalin ACell culturebiology.proteinChondrilla nuculaAntiviral Chemistry and Chemotherapy
researchProduct

Cytostatic Activity of Aeroplysinin-1 against Lymphoma and Epithelioma Cells

1989

(±)-Aeroplysinin-1, an optically active 1.2-dihydroarene-1.2-diol. was isolated from the marine sponges Verongia aerophoba (+-isomer) and lanthella ardis (--isomer). For the experiments presented we used the +-isomer from Verongia aerophoba. Here we describe the hitherto unknown biological and pharmacological property of this compound to display pronounced anticancer activity against L5178y mouse lymphoma cells (ED50: 0.5 μm). Friend erythroleukemia cells (ED50: 0.7μm) , human mamma carcinoma cells (ED50: 0.3μm) and human colon carcinoma cells (ED50: 3.0 μm) in vitro. Furthermore, aeroplysinin caused a preferential inhibition of [3H]thymidine (dThd) incorporation rates in L5178y mouse lymph…

MaleSalmonella typhimuriumAcetonitrilesCell SurvivalCellAntineoplastic AgentsMice Inbred StrainsBiologyGeneral Biochemistry Genetics and Molecular BiologyCell LineMicechemistry.chemical_compoundIn vivoCyclohexenesTumor Cells CulturedmedicineCarcinomaAnimalsHumansLeukemia L5178ED50Leukemia ExperimentalMutagenicity TestsMelanomaCarcinomamedicine.diseaseVirologyMolecular biologyIn vitroLymphomamedicine.anatomical_structurechemistryDrug Screening Assays AntitumorThymidineZeitschrift für Naturforschung C
researchProduct