Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

English (EN)·Polski (PL)·Yкраїнський (UK)
Przejdź do strony domowej biblioteki Centralna Biblioteka Wojskowa Link otwiera się w nowym oknie Logo biblioteki Prolib Integro - strona głównaCentralna Biblioteka Wojskowa

Wyszukujesz frazę "glycoproteins" wg kryterium: Temat

  Lista filtrów
Wyrównaj
    Wyświetlanie 1-7 z 7
    Tytuł:
    Structure and biosynthesis of human salivary mucins.
    Autorzy:
    Zalewska, Anna
    Zwierz, Krzysztof
    Żółkowski, Krzysztof
    Gindzieński, Andrzej
    Powiązania:
    https://bibliotekanauki.pl/articles/1044229.pdf
    Data publikacji:
    2000
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    glycoproteins
    human
    saliva
    mucins
    Opis:
    Human salivary glands secrete two types of mucins: oligomeric mucin (MG1) with molecular mass above 1 MDa and monomeric mucin (MG2) with molecular mass of 200-250 kDa. Monomers of MG1 and MG2 contain havily O-glycosylated tandem repeats located at the central domain of the molecules. MG1 monomers are linked by disulfide bonds located at sparsely glycosylated N- and C-end. MG1 are synthesized by mucous cells and MG2 by the serous cells of human salivary glands.
    Źródło:
    Acta Biochimica Polonica; 2000, 47, 4; 1067-1079
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Comparative biochemical analysis of lectin and nuclease from Chelidonium majus L.
    Autorzy:
    Fik, Ewa
    Dalgalarrondo, Michele
    Haertlé, Thomas
    Goździcka-Józefiak, Anna
    Powiązania:
    https://bibliotekanauki.pl/articles/1044368.pdf
    Data publikacji:
    2000
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    glycoproteins
    glycosylation
    plant lectins
    Chelidonium majus
    Opis:
    It has been recently recognized that lectins exhibit other activities besides hemagglutination. Previously we have found that purified lectin from Chelidonium majus showed DNase activity (Fik, Goździcka-Józefiak & Kędzia, 1995, Herba Polon. 41, 84-95). Comparison of lectin and DNase from the sap from leaves and roots of Chelidonium majus proved that both these compounds are composed of 24 kDa monomer subunits which have an identical N-terminal sequence but differ in amino-acid composition and degree of glycosylation. Possible interrelationship between lectin and DNase is discussed.
    Źródło:
    Acta Biochimica Polonica; 2000, 47, 2; 413-420
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    A biochemical study on the level of lipids and glycoproteins in the serum and platelets of liver cirrhotic bleeders
    Autorzy:
    Vijayalakshmi, Sivagurunathan
    Geetha, Arumugam
    Jeyachristy, Sam
    Powiązania:
    https://bibliotekanauki.pl/articles/1041294.pdf
    Data publikacji:
    2006
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    glycoproteins
    lipids
    cirrhosis
    adenosine triphosphatases
    platelets
    Opis:
    Bleeding complication and abnormal platelet functions are associated with liver cirrhosis. The aim of the present investigation was to assess the functional integrity of platelets in terms of lipids like cholesterol and phospholipids, glycoproteins and membrane-bound enzymes. Liver cirrhotic patients with bleeding complications were studied. Age and sex matched normal healthy volunteers were also involved in this study as a control group. Levels of cholesterol, phospholipids, glycoproteins and adenosine triphosphatases were assessed in isolated platelet membrane fraction. The level of glycoproteins and the activity of adenosine triphosphatases were found to be decreased significantly in cirrhotic patients. The cholesterol/phospholipid ratio was found to be altered significantly, indicating an alteration in the fluidity of platelet membrane. The results of this study reveal that the functional impairment of platelets in liver cirrhotic patients which is responsible for their bleeding tendency might also be due to altered lipid and enzyme levels in platelet membrane.
    Źródło:
    Acta Biochimica Polonica; 2006, 53, 1; 213-220
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Effect of N-glycosylation inhibition on the synthesis and processing of classical swine fever virus glycoproteins
    Autorzy:
    Tyborowska, Jolanta
    Zdunek, Ewa
    Szewczyk, Bogusław
    Powiązania:
    https://bibliotekanauki.pl/articles/1040876.pdf
    Data publikacji:
    2007
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    glycoproteins
    pestivirus
    glycosylation
    classical swine fever virus
    Opis:
    Classical swine fever virus (CSFV) is often used as a surrogate model in molecular studies of the closely related hepatitis C virus. In this report we have examined the effect of the inhibition of glycosylation on the survival and maturation of CSFV. Viral glycoproteins (Erns, E1, E2) form biologically active complexes - homo- and heterodimers, which are indispensable for viral life cycle. Those complexes are highly N-glycosylated. We studied the influence of N-glycosylation on dimer formation using Erns and E2 glycoproteins produced in insect cells after infection with recombinant baculoviruses. The glycoproteins were efficiently synthesized in insect cells, had similar molecular masses and formed dimers like their natural counterparts. Surprisingly, the addition of tunicamycin (an antibiotic which blocks early steps of glycosylation) to insect cell culture blocked not only dimer formation but it also led to an almost complete disappearance of E2 even in monomeric form. Tunicamycin did not exert a similar effect on the synthesis and formation of Erns dimers; the dimers were still formed, which suggests that Erns glycan chains are not necessary for dimer formation. We have also found that very low doses of tunicamycin (much lower than those used for blocking N-glycosylation) drastically reduced CSFV spread in SK6 (swine kidney) cell culture and the virus yield. These facts indicate that N-glycosylation inhibitors structurally similar to tunicamycin may be potential therapeutics for the inhibition of the spread of CSFV and related viruses.
    Źródło:
    Acta Biochimica Polonica; 2007, 54, 4; 813-819
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Effect of tunicamycin on the biogenesis of hepatitis C virus glycoproteins
    Autorzy:
    Reszka, Natalia
    Krol, Ewelina
    Patel, Arvind
    Szewczyk, Boguslaw
    Powiązania:
    https://bibliotekanauki.pl/articles/1040320.pdf
    Data publikacji:
    2010
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    glycoproteins
    glycosylation inhibition
    hepatitis C virus
    tunicamycin
    Opis:
    Hepatitis C virus (HCV) infects humans, with a prevalence around 3% of population, causing acute and chronic hepatitis and hepatocellular carcinoma. We studied the effect of inhibition of glycosylation on the assembly of the HCV particle. HCV possesses two envelope glycoproteins E1 and E2 that are highly modified by N-glycans. These glycan residues are crucial for viral entry and maturation of the progeny. Here, we examined the influence of inhibition of N-glycosylation on expression of E1 and E2. Since the propagation of HCV in cell culture is limited, we used a recombinant baculovirus producing viral-like particles in insect cells. Our data showed that blocking of N-glycan transfer to the nascent polypeptide chain with the antibiotic tunicamycin resulted in the loss of E1 and E2. We also found that a dose of tunicamycin that did not influence the cell viability significantly reduced the E2 level in infected cells. The results indicate that blocking of glycosylation at an early step efficiently reduces the assembly of HCV virions. Thus, we suggest that derivatives of tunicamycin that preferentially block glycosylation of viral proteins may become potential therapeutic agents against HCV.
    Źródło:
    Acta Biochimica Polonica; 2010, 57, 4; 541-546
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Interaction of glycophorin A with lectins as measured by surface plasmon resonance (SPR).
    Autorzy:
    Krotkiewska, Bożena
    Pasek, Marta
    Krotkiewski, Hubert
    Powiązania:
    https://bibliotekanauki.pl/articles/1043786.pdf
    Data publikacji:
    2002
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    glycoproteins
    surface plasmon resonance
    lectins
    human glycophorin
    biosensor
    Opis:
    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 BIAcoreTM 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.
    Źródło:
    Acta Biochimica Polonica; 2002, 49, 2; 481-490
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    High performance liquid chromatography and photodiode array detection of ferulic acid in Rubus protoplasts elicited by O-glycans from Fusarium sp. M7-1.
    Autorzy:
    Nita-Lazar, Mihai
    Chevolot, Lionel
    Iwahara, Shojiro
    Takegawa, Kaoru
    Furmanek, Aleksandra
    Lienart, Yvette
    Powiązania:
    https://bibliotekanauki.pl/articles/1043710.pdf
    Data publikacji:
    2002
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    phenylalanine-ammonia lyase
    Rubus protoplasts
    Fusarium glycoproteins
    O-glycan signal
    Opis:
    So far only little data have been available concerning the eliciting capacity of well defined glycan molecules isolated from plant pathogens. This study brings new information about changes in plant cells caused by fungal pathogens. Sugar fractions derived from glycoproteins isolated from the fungus Fusarium sp. M7-1 have been tested here as signaling molecules. The ability of three O-glycan fractions (named in this work inducer I, II, III) to trigger responses in Rubus protoplasts has been examined. It was found that inducer III was the most efficient as it elicited changes in the levels of phenylpropanoid pathway intermediates in relation to phenylalanine-ammonia lyase (PAL) activation.
    Źródło:
    Acta Biochimica Polonica; 2002, 49, 4; 1019-1027
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-7 z 7

      Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies