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Wyszukujesz frazę "lectin" wg kryterium: Temat


Wyświetlanie 1-9 z 9
Tytuł:
Analysis of surface carbohydrates of Eudiplozoon nipponicum [Monogenea, Diplozoidae] using lectin binding techniques
Autorzy:
Hricova, I.
Horak, P.
Gelnar, M.
Koubkova, B.
Powiązania:
https://bibliotekanauki.pl/articles/840825.pdf
Data publikacji:
1998
Wydawca:
Polskie Towarzystwo Parazytologiczne
Tematy:
lectin
Diplozoidae
Eudiplozoon nipponicum
surface
Monogenea
carbohydrate
Źródło:
Annals of Parasitology; 1998, 44, 3
0043-5163
Pojawia się w:
Annals of Parasitology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Structural studies of algal lectins with anti-HIV activity
Autorzy:
Ziółkowska, Natasza
Wlodawer, Alexander
Powiązania:
https://bibliotekanauki.pl/articles/1041149.pdf
Data publikacji:
2006
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
topical antivirals
protein structure
HIV
lectin
AIDS
Opis:
A number of antiviral lectins, small proteins that bind carbohydrates found on viral envelopes, are currently in pre-clinical trials as potential drugs for prevention of transmission of human immunodeficiency virus (HIV) and other enveloped viruses, such as the Ebola virus and the coronavirus responsible for severe acute respiratory syndrome (SARS). Lectins of algal origin whose antiviral properties make them candidate agents for prevention of viral transmission through topical applications include cyanovirin-N, Microcystis viridis lectin, scytovirin, and griffithsin. Although all these proteins exhibit significant antiviral activity, their structures are unrelated and their mode of binding of carbohydrates differs significantly. This review summarizes the current state of knowledge of the structures of algal lectins, their mode of binding of carbohydrates, and their potential medical applications.
Źródło:
Acta Biochimica Polonica; 2006, 53, 4; 617-626
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
A novel tetrameric lectin from Lycoris aurea with four mannose binding sites per monomer
Autorzy:
Liu, Jiwei
Xu, Xiaochao
Liu, Jinzhi
Balzarini, Jan
Luo, Yongtin
Kong, Yang
Li, Jian
Chen, Fang
Van Damme, Els
Bao, Jinku
Powiązania:
https://bibliotekanauki.pl/articles/1041131.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
sequence alignment
mannose-binding lectin
Lycoris aurea agglutinin
molecular modeling and docking
Opis:
The mannose-binding agglutinin from bulbs of Lycoris aurea (LAA) agglutinates rabbit but not human erythrocytes. The molecular mass of the monomer in SDS/PAGE is 12 kDa while the apparent molecular mass in gel filtration is 48 kDa, indicating that LAA is a homotetramer. The full-length cDNA of LAA contains 683 bp with an open reading frame encoding a protomer of 162 amino-acid residues. Hydrophobic Cluster Analysis and molecular modeling of the 109-residue mature polypeptide suggested a similar secondary and tertiary structure to those of Narcissus pseudonarcissus agglutinin (NPA). Molecular docking revealed that, besides the three mannose-binding sites common among Amaryllidaceae lectins, LAA also contains a fourth unique mannose-binding site formed by a tryptophan cluster. The existence of four mannose-binding sites in each monomer of LAA is very unusual and has only been reported for NPA earlier.
Źródło:
Acta Biochimica Polonica; 2007, 54, 1; 159-166
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
A novel lectin with antiproliferative activity from the medicinal mushroom Pholiota adiposa
Autorzy:
Zhang, G.
Sun, J.
Wang, H.
Ng, T.
Powiązania:
https://bibliotekanauki.pl/articles/1040531.pdf
Data publikacji:
2009
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Pholiota adiposa
lectin
mushroom
purification
antiproliferative
Opis:
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 50°C, 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.
Źródło:
Acta Biochimica Polonica; 2009, 56, 3; 415-421
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Novel galactonic acid-binding hexameric lectin from Hibiscus mutabilis seeds with antiproliferative and potent HIV-1 reverse transcriptase inhibitory activities
Autorzy:
Lam, Sze
Ng, Tzi
Powiązania:
https://bibliotekanauki.pl/articles/1040480.pdf
Data publikacji:
2009
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Hibiscus mutabilis
hexameric lectin
galactonic acid
Opis:
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 50°C, 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.
Źródło:
Acta Biochimica Polonica; 2009, 56, 4; 649-654
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Occurrence and biological activity of lectins in seeds of leguminous plants and cereals
Występowanie i aktywność biologiczna lektyn w nasionach roślin strączkowych i ziarnach zbóż
Autorzy:
Brinken, A.
Piatek, J.
Biel, W.
Sagan, Z.
Powiązania:
https://bibliotekanauki.pl/articles/82538.pdf
Data publikacji:
2012
Wydawca:
Zachodniopomorski Uniwersytet Technologiczny w Szczecinie. Wydawnictwo Uczelniane ZUT w Szczecinie
Tematy:
occurrence
biological activity
lectin
seed
leguminous plant
cereal grain
agglutination
ram
rat
man
blood
erythrocyte
feed
hemagglutination test
mushroom
Agaricus campestris
Źródło:
Folia Pomeranae Universitatis Technologiae Stetinensis. Agricultura, Alimentaria, Piscaria et Zootechnica; 2012, 24
2081-1284
Pojawia się w:
Folia Pomeranae Universitatis Technologiae Stetinensis. Agricultura, Alimentaria, Piscaria et Zootechnica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Pinellia ternata agglutinin produced in Bombyx mori cells exhibits bioactivity
Autorzy:
Xu, Tao
Wang, Bo
Wang, Liya
Zhang, Yaozhou
Lv, Zhengbing
Powiązania:
https://bibliotekanauki.pl/articles/1039738.pdf
Data publikacji:
2012
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Pinellia ternata agglutinin
silkworm bioreactor
plant lectin
Bombyx mori cells
Opis:
Pinellia ternata agglutinin (PTA) is highly homologous to many other monocot mannose-binding lectins which reportedly possess antitumor activities. Its production in silkworm cells has great application potential because the baculovirus expression system can produce post-translationally modified proteins at low cost. In the current study, the pta gene was cloned and expressed in silkworm cells, and the expressed protein was analyzed using a hemagglutination assay. A preliminary in vitro study on its anti-proliferative activity was performed. The results show that the recombinant PTA with an apparent molecular mass of 29 kDa can hemagglutinate rabbit erythrocytes and this activity can be inhibited by D-mannan at a low concentration. In addition, the recombinant hemagglutinin exhibited a dose-dependent anti-proliferative activity on hepatoma cells. The results of the current study suggest that PTA and other important bioactive proteins could be produced by silkworm bioreactor for biomedicine research and application.
Źródło:
Acta Biochimica Polonica; 2012, 59, 2; 231-236
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Naturalne substancje pochodzenia roślinnego negatywnie oddziałujące na zdrowie krów oraz jakość mleka
Natural substances of plant origin adeversely affecting health of cows and milk quality
Autorzy:
Brodziak, A.
Krol, J.
Nowaczek, A.
Powiązania:
https://bibliotekanauki.pl/articles/828600.pdf
Data publikacji:
2017
Wydawca:
Polskie Towarzystwo Technologów Żywności
Tematy:
toksyny roslinne
mikotoksyny
pasze przemyslowe
mleko
system wczesnego ostrzegania o niebezpiecznych produktach zywnosciowych i srodkach zywienia zwierzat
alkaloidy
glikozydy
saponiny
olejki eteryczne
kwasy organiczne
toksyny
grzyby plesniowe
glukozynolany
kumaryna
furanokumaryny
lektyny
fitoestrogeny
zagrozenia zdrowia
krowy
plant
toxin
mycotoxin
feed
milk
RASFF system
alkaloid
glycoside
saponin
essential oil
organic acid
mould
glucosinolate
coumarin
furanocoumarin
lectin
phytoestrogen
health risk
cow
Opis:
Celem pracy było omówienie zagrożeń dla zdrowia zwierząt wywołanych przez naturalne substancje szkodliwe, tj. fitotoksyny i mikotoksyny pochodzące z pasz, z uwzględnieniem ich negatywnego wpływu na jakość mleka, a w konsekwencji na zdrowie człowieka. Jako najbardziej szkodliwe związki pochodzące z pasz najczęściej wymieniane są: alkaloidy, glikozydy, saponiny, olejki eteryczne i kwasy organiczne, a także toksyny produkowane przez grzyby pleśniowe. Mniejszą szkodliwością charakteryzują się natomiast: glukozynolany, kumaryny i pochodne furanokumaryny, lektyny, a także fitoestrogeny. Zarówno związki szkodliwe występujące naturalnie w zielonce i w innych paszach objętościowych, jak również mikotoksyny stanowią potencjalne zagrożenie dla zdrowia i życia zwierząt, oddziałując na ich produkcyjność, jak też na jakość surowców, w tym mleka. Największe zagrożenie dla zdrowia zwierząt i ludzi stanowi aflatoksyna B₁ z uwagi na jej udowodnione działanie kancerogenne i mutagenne. Jak wskazują raporty z systemu RASFF, rzadko dochodzi jednak do wystąpienia tego typu zagrożeń. Wynika to z selektywnego pobierania paszy przez zwierzęta, zwłaszcza wypasane, jak również z działań podejmowanych przez hodowców w ramach Dobrych Praktyk Rolniczych.
The objective of the research study was to discuss risks to animal health caused by natural harmful substances, i.e. phytotoxins and mycotoxins derived from feed in view of their adverse impact on milk quality and, consequently, on human health. As the most harmful compounds derived from feed are commonly indicated alkaloids, glycosides, saponins, essential oils, and organic acids as well as toxins produced by mould. Less harmful are glucosinolates, coumarin and derivatives of furanocoumarin, lectins, and, also, phytoestrogens. Both the harmful compounds naturally occurring in fresh forage and in other bulky feeds and the mycotoxins are a potential threat to health and life of animals since they affect productivity of animals as well as the quality of raw materials including milk. The biggest threat to animal and human health is aflatoxin B₁ because of its proven carcinogenic and mutagenic effects. However, as it is indicated by RASFF reports, such risks rarely occur. It results from two facts: animals selectively take and consume feed, particularly the grazing animals; farmers take actions under the Good Agricultural Practices.
Źródło:
Żywność Nauka Technologia Jakość; 2017, 24, 1
1425-6959
Pojawia się w:
Żywność Nauka Technologia Jakość
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Antimicrobial activities and phylogenetic study of Erythrina senegalensis DC (Fabaceae) seed lectin
Autorzy:
Enoma, Samuel
Adewole, Taiwo S.
Agunbiade, Titilayo O.
Kuku, Adenike
Powiązania:
https://bibliotekanauki.pl/articles/16672367.pdf
Data publikacji:
2023
Wydawca:
Polska Akademia Nauk. Czasopisma i Monografie PAN
Tematy:
antimicrobial
Erythrina senegalensis
lectin
phylogenetic analysis
polymerase chain reaction
Opis:
Erythrina senegalensis (Fabaceae) have been traditionally used in the treatment of microbial ailments, and the specific agent mediating its efficacy has been investigated in several studies. In this study, the antimicrobial activity of purified E. senegalensis lectin (ESL) was analyzed. The phylogenetic relationship of the gene encoding lectin with other legume lectins was also established to investigate their evolutionary relationship via comparative genomics. Antimicrobial activity of ESL against selected pathogenic bacteria and fungi isolates was evaluated by the agar well diffusion method, using fluconazole (1 mg/ml) and streptomycin (1 mg/ml) as positive controls for fungi and bacteria sensitivity, respectively. Potent antimicrobial activity of ESL against Erwinia carotovora, Pseudomonas aeruginosa, Klebsiella pneumonia, Staphylococcus aureus, Aspergillus niger, Penicillium camemberti, and Scopulariopsis brevicaulis was observed, with inhibition zones ranging from 18 to 24 mm. Minimum inhibitory concentrations of ESL ranged between 50 and 400 μg/ml. Primer-directed polymerase chain reaction of E. senegalensis genomic DNA detected a 465-bp lectin gene with an open reading frame encoding a 134-amino acid polypeptide. The obtained nucleotide sequence of the ESL gene shared high sequence homology: 100, 100, and 98.18% with Erythrina crista-galli, Erythrina corallodendron, and Erythrina variegata lectin genes, respectively, suggesting that the divergence of Erythrina lectins might follow species evolution. This study concluded that ESL could be used to develop lectin-based antimicrobials, which could find applications in the agricultural and health sectors.
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2023, 104, 1; 21-32
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-9 z 9

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