Wyniki wyszukiwania

1

Application of fluorescein-labelled lectins with different glycan-binding specificities to the studies of cellular glycoconjugates in human full-term placenta

100%

Konska G., Zamorska L., Pituch-Noworolska A., Szmaciarz M., Guillot J.

Folia Histochemica et Cytobiologica

|

2003

|

tom 41

|

nr 3

2

Lectins in plant reproductive organs

88%

Kovaleva L., Komarova E.

Acta Biologica Cracoviensia. Series Botanica. Supplement

|

1999

|

tom 41

|

nr 1

3

Possible participation of lectins in cold adaptation of winter wheat

88%

Komarova E. N., Trunova T. I.

Biological Bulletin of Poznań. Supplement

|

1997

|

tom 34

4

Neoglycoconjugates - a tool for conjugation of carbohydrates with liposomes

88%

Boratynski J.

Cellular and Molecular Biology Letters

|

1999

|

tom 04

|

nr 2

5

Histological changes in mouse thymus after intraperitoneal injection of Robinia pseudoacacia L. (RpA) lectin

75%

Pierscinski A., Zaremba S., Banach M.

Acta Biologica Cracoviensia. Series Zoologia

|

1989

|

tom 31

6

Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik

Antimicrobial activities and phylogenetic study of Erythrina senegalensis DC (Fabaceae) seed lectin

75%

Enoma S., Adewole T. S., Agunbiade T. O., Kuku A.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

|

2023

|

tom 104

|

nr 1

7

Effect of lectin from Chelidonium majus L. on normal and cancer cells in culture

75%

Fik E., Wolun-Cholewa M., Kistowska M., Warchol J. B., Gozdzicka-Jozefiak A.

Folia Histochemica et Cytobiologica

|

2001

|

tom 39

|

nr 2

8

Age-related profile of beta-N-acetylhexosaminidase glycosylation in rat liver

75%

Litynska A., Przybylo M.

Acta Biochimica Polonica

|

1998

|

tom 45

|

nr 3

β-N-acetylhexosaminidase was prepared from a liver lysosomal fraction obtained from rats between 18 days of gestation (group I) and 72 weeks of age (groups II-VI). A glycan chain analysis was performed after an electrophoresis and blotting, followed by a very sensitive detection system with highly specific digoxigenin-labelled lectins. The presence of high-mannose /hybrid type glycans, as well as their fucosylated forms was shown in all the experimental groups. Complex-type glycans with terminal sialic acid or galactose were present in all the groups except for 1-week-old rats in which only a positive reaction with lectins from Galanthus nivalis and Aleuria aurantia - was observed. Thus it may be assumed that age-related changes in the glycosylation pattern occur on the first days after birth.

9

The carbohydrate moiety of human glycophorin in CDG syndrome

75%

Krotkiewska B., Zwierz K., Krotkiewski H.

Acta Biochimica Polonica

|

1999

|

tom 46

|

nr 2

Human glycophorin, the major sialoglycoprotein of erythrocyte membranes, was isolated from erythrocytes of healthy individuals and four patients with CDG syndrome. Sugar analysis revealed lower carbohydrate content in three out of four CDG-glycophorin samples. In order to characterize closer the glycosylation differences between glycophorin samples in health and disease, reaction with four biotinylated lectins was performed, using ELISA procedure on polystyrene microplates. Results obtained so far strongly suggest that both N- and O-glycans of glycophorin are affected in CDG syndrome.

10

Interaction of glycophorin A with lectins as measured by surface plasmon resonance [SPR]

75%

Krotkiewska B., Pasek M., Krotkiewski H.

Acta Biochimica Polonica

|

2002

|

tom 49

|

nr 2

Glycophorin A (GPA), the major sialoglycoprotein of the human erythrocyte membrane, was isolated from erythrocytes of healthy individuals of blood groups A, B and O using phenol-water extraction of erythrocyte membranes. Interaction of individual GPA samples with three lectins (Psathyrella velutina lectin, PVL; Triticum vulgaris lectin, WGA and Sambucus nigra I agglutinin SNA-I) was analyzed using a BIAcore™ biosensor equipped with a surface plasmon resonance (SPR) detector. The experiments showed no substantial differences in the interaction between native and desialylated GPA samples originating from erythrocytes of either blood group and each of the lectins. Desialylated samples reacted weaker than the native ones with all three lectins. PVL reacted about 50-fold more strongly than WGA which, similar to PVL, recognizes GlcNAc and Neu5Ac residues. SNA-I lectin, recognizing α2-6 linked Neu5Ac residues, showed relatively weak reaction with native and only residual reaction with desialylated GPA samples. The data obtained show that SPR is a valuable method to determine interaction of glycoproteins with lectins, which potentially can be used to detect differences in the carbohydrate moiety of individual glycoprotein samples.

11

Immunocytochemical localization of lectin in cotyledons of developing seedlings of Cucurbita ficifolia

75%

Lorenc-Kubis I., Bonfante P.

Acta Biochimica Polonica

|

1994

|

tom 41

|

nr 2

12

Analysis of surface carbohydrates of Eudiplozoon nipponicum [Monogenea, Diplozoidae] using lectin binding techniques

75%

Hricova I., Horak P., Gelnar M., Koubkova B.

Wiadomości Parazytologiczne

|

1998

|

tom 44

|

nr 3

13

Lectins from squash [Cucurbita ficifolia] seedlings

75%

Lorenc-Kubis I., Klimczak A., Morawiecka B.

Acta Biochimica Polonica

|

1993

|

tom 40

|

nr 1

14

How endothelial cell organo-specificity mediates circulating cell homing

75%

Kieda C.

Archivum Immunologiae et Therapiae Experimentalis

|

2003

|

tom 51

|

nr 2

15

GalNAc-Gal specific lectin from German iris [Iris germanica L.] rootstock

75%

Ferens-Sieczkowska M., Morawiecka B.

Acta Biochimica Polonica

|

1993

|

tom 40

|

nr 1

16

Developmental differences in acid phosphatase and agglutination activity in roots of Cucurbita ficifolia seedlings. Purification and some properties of lectin

75%

Lorenc-Kubis I., Krawcow A., Morawiecka B.

Acta Biochimica Polonica

|

1994

|

tom 41

|

nr 2

17

Subtle differences in glycosylation of blood group M and N type glycophorin A detected with anti-Tn lectins and confirmed by chemical analysis

75%

Krotkiewski H., Duk M., Lisowska E.

Acta Biochimica Polonica

|

1995

|

tom 42

|

nr 1

A higher content of Tn and sialyl-Tn receptors in glycophorin A of blood group N than in that of blood group M was suggested by reactions with anti-Tn lectins. Analysis of [^-elimination products of two blood group M and two blood group N preparations by gas liquid chromatography-mass spectrometry showed that GalNAc- -ol was detectable in minor amounts in all analyzed samples and its content was higher in the products obtained from desialylated antigens. Moreover, the content of Gal N Ac- -ol detected in blood group N samples was almost twice as high as in respective blood group M samples. Since blood group M and N antigens differ in two amino-acid residues, our results support the existence of sequence-dependent differences in efficiency of substitution of glycophorin GalNAc-Ser/Thr residues with galactose.

18

Novel galactonic acid-binding hexameric lectin from Hibiscus mutabilis seeds with antiproliferative and potent HIV-1 reverse transcriptase inhibitory activities

63%

Lam S. K., Ng T. B.

Acta Biochimica Polonica

|

2009

|

tom 56

|

nr 4

649-654

A hexameric 150-kDa lectin was isolated from dried Hibiscus mutabilis seeds using a chromatographic protocol that involved ion exchange chromatography on SP-Sepharose, and gel filtration on Superdex 75 and Superdex 200. The lectin was not adsorbed on SP-Sepharose and was eluted from the Superdex 75 column in the void volume. It was eluted in the first peak from Superdex 200. It was strongly adsorbed on DEAE-cellulose and Q-Sepharose and could not be easily desorbed. The hemagglutinating activity of the lectin, which was stable at pH 4-7 and up to 50oC, could be inhibited by 25 mM galactonic acid. This is the first report of a galactonic acid-binding lectin. It potently inhibited HIV-1 reverse transcriptase with an IC50 of 0.2 µM. It exhibited weak antiproliferative activity towards both hepatoma HepG2 cells (40% inhibition) and breast cancer MCF-7 cells (50% inhibition) at 100 µM concentration of the lectin. It did not inhibit mycelial growth of a number of fungi tested.

19

A novel lectin with antiproliferative activity from the medicinal mushroom Pholiota adiposa

63%

Zhang G. Q., Sun J., Wang H. X., Ng T. B.

Acta Biochimica Polonica

|

2009

|

tom 56

|

nr 3

415-421

Little was known about biological activities of compounds from the medicinal mushroom of the genus Pholiota. A lectin from the Pholiota adiposa has now been isolated and its properties tested. The isolation procedure included ion exchange chromatography on DEAE-cellulose and CM-cellulose, and fast protein liquid chromatography-gel filtration (FPLC) on Superdex 75. The lectin was composed of two identical subunits, each with a molecular mass of 16 kDa. Its N-terminal amino-acid sequence showed little similarity to sequences of other Agaricales lectins. The hemagglutinating activity of the lectin was stable at temperatures up to 50oC, and in NaOH and HCl solutions with concentrations less than 25 mM. It was inhibited by inulin (12.5-200 mM), but enhanced by Cu2+ (6.25-25 mM), Fe2+ (12.5-25 mM), and Al3+ (6.25-25 mM) ions. The lectin showed antiproliferative activity toward hepatoma Hep G2 cells and breast cancer MCF7 cells with an IC50 of 2.1 μM and approximately 3.2 μM, respectively. It exhibited HIV-1 reverse transcriptase inhibitory activity with an IC50 of 1.9 μM. When compared with P. aurivella lectin, the only Pholiota lectin published to date, P. adiposa lectin differs in chromatographic behavior, molecular mass, N-terminal sequence, and effect of cations on hemagglutinating activity. In the case of the lectin from P. aurivella, its antifungal, antiproliferative, and HIV-1 reverse transcriptase inhibitory activities have not been determined.

20

Analysis of recombinant Duffy protein-linked N-glycans using lectins and glycosidases

63%

Grodecka M., Czerwinski M., Duk M., Lisowska E., Wasniowska K.

Acta Biochimica Polonica

|

2010

|

tom 57

|

nr 1

49-53

Duffy antigen is a glycosylated blood group protein acting as a malarial and chemokine receptor. Using glycosylation mutants we have previously demonstrated, that all three potential glycosylation sites of the Duffy antigen are occupied by N-linked oligosaccharide chains. In this study, wild-type Duffy glycoprotein and three mutants, each containing a single N-glycan, were used to characterize the oligosaccharide chains by lectin blotting and endoglycosidase digestion. The positive reaction of all the recombinant Duffy forms with Datura stramonium and Sambucus nigra lectins showed that each Duffy N-linked glycan contains Galβ1-4GlcNAc units terminated by (α2-6)-linked sialic acid residues, typical of complex oligosaccharides. The reactivity with Aleuria aurantia and Lens culinaris lectins suggested the presence of (α1-6)-linked fucose at the N-glycan chitobiose core. The failure of the Galanthus nivalis and Canavalia ensiformis lectins to bind to any of the Duffy mutants or to the wild-type antigen indicated that none of the three Duffy N-glycosylation sites carries detectable levels of high-mannose oligosaccharide chains. Digestion of Duffy samples with peptide N-glycosidase F and endoglycosidase H confirmed the presence of N-linked complex oligosaccharides. Our results indicate that Duffy antigen N-glycans are mostly core-fucosylated complex type oligosaccharides rich in N-acetyllactosamine and terminated by (α2-6)-linked sialic acid residues.

Ograniczanie wyników

Application of fluorescein-labelled lectins with different glycan-binding specificities to the studies of cellular glycoconjugates in human full-term placenta

Lectins in plant reproductive organs