Preferencje help
Polish version English version Język
Widoczny [Schowaj] Abstrakt
Liczba wyników

Znaleziono wyników: 9

Liczba wyników na stronie
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników

Wyniki wyszukiwania

help Sortuj według:

help Ogranicz wyniki do:
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
1

Mucyny ludzkie przewodu pokarmowego jako produkty genow MUC

100%
Paszkiewicz-Gadek A., Porowska H.
Postępy Higieny i Medycyny Doświadczalnej
|
2000
|
tom 54
|
nr 2
183-198
2

Activity of partially purified UDP-N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase with different peptide acceptors

80%
Porowska H., Paszkiewicz-Gadek A., Gindzienski A.
Acta Biochimica Polonica
|
1999
|
tom 46
|
nr 2
As part of investigations on the role of the UDP-GalNAc-ribosome complex in the initial O-glycosylation of proteins, we have isolated from porcine gastric mucosa GalNAc-transferase, mucin and apomucin, and its three fractions containing carbohydrate in the amounts: I - 1.6%, II - 0.65% and III - 0.00% (wt/wt) of apomucin mass. Amino acid analysis showed that fractions I and II contained slightly higher amounts of serine and threonine as compared to native mucin and apomucin. The short peptide Pro-Thr-Ser-Ser-Pro-Ile-Ser-Thr was the most effectively glycosylated. Our apomucin preparations are also good acceptors of GalNAc and can be used for testing of O-glycosylation in vitro.
3

The participation of ribosomes in protein glycosylation. Interaction of the ribosome-UDP-N-acetyl-glucosamine complex with dolichol phosphate

80%
Paszkiewicz-Gadek A., Porowska H., Galasinski W.
Acta Biochimica Polonica
|
1992
|
tom 39
|
nr 3
UDP-N-acetylglucosaminc can be bound by pure ribosomes. The part of N-acetylglucosamine-1-P can be transferred from the complex ribosome-UDP-N-acetylglucosamine onto dolichol phosphate. Evidence Is presented that N-acetylglucosamine bound to dolichol phosphate can be transferred to the nascent peptide synthesized on the ribosomc.
4

The participation of ribosome-UDP-GalNAc complex in the initiation of protein glycosylation in vitro

80%
Paszkiewicz-Gadek A., Porowska H., Gindzienski A.
Acta Biochimica Polonica
|
2000
|
tom 47
|
nr 2
The gastric epithelial cells ribosome-UDP-GalNAc complex is a donor of UDP- GalNAc as the substrate for N-acetylgalactosaminyltransferase, which catalyse the transfer of GalNAc residue to the polypeptide, existing on polysomes. It was observed that the deglycosylated porcine mucin and synthetic peptide (PTSSPIST) can be also glycosylated with participation of N-acetylgalactosaminyltransferase and ribosome- UDP-GalNAc complex. The probability of the ribosome-UDP-GalNAc complex as an intermediate in the O-glycosylation is considered.
5

The influence of brefeldin on MUC1 expression and adhesive properties of carcinoma cell lines

71%
Porowska H., Paszkiewicz-Gadek A., Pietruszczuk M., Wolczynski S., Gindzienski A.
Acta Biochimica Polonica
|
2006
|
tom 53
|
nr Supplement 1
6

Transmembrane glycoprotein MUC1 in epithelium of human placenta after normal partus

71%
Paszkiewicz-Gadek A., Porowska H., Wosek J., Gindzienski A., Kobylec E.
Acta Biochimica Polonica
|
2006
|
tom 53
|
nr Supplement 1
7

The levels of sMUC-1 in patients with multiple myeloma

61%
Lemancewicz D., Bolkun L., Porowska H., Galar M., Semeniuk J., Kloczko J., Dzieciol J.
Folia Histochemica et Cytobiologica
|
2011
|
tom 49
|
nr 4
8

Expression of MUC1 mucin in human umbilical vein endothelial cells (HUVEC)

61%
Porowska H., Paszkiewicz-Gadek A., Wosek J., Wnuczko K., Rusak M., Szczepanski M.
Folia Histochemica et Cytobiologica
|
2010
|
tom 48
|
nr 3
9

Glutathione reductase activity correlates with concentration of extracellular matrix degradation products in synovial fluid from patients with joint diseases

61%
Sredzinska K., Galicka A., Porowska H., Sredzinski L., Porowski T., Popko J.
Acta Biochimica Polonica
|
2009
|
tom 56
|
nr 4
635-640
 The mechanisms underlying cartilage matrix degradation in joint diseases is not fully understood but reactive oxygen species are implicated as main causative factors. Comparative studies of glutathione reductase (GR) activity in synovial fluid from patients with rheumatoid arthritis (RA), reactive arthritis (ReA) and osteoarthritis (OA) as well as correlations between GR activity and concentration of the major cartilage components in synovial fluid are presented in this study. We found significantly higher activity of GR in RA (about three-fold) and ReA (about two-fold) than in OA. In RA and ReA patients, GR activity in synovial fluid correlates negatively with the concentrations of collagen and degradation products of sulfated glycosaminoglycans. In OA patients the activity of GR was significantly lower than in RA and ReA, which positively correlated with the concentration of collagen and showed a tendency for positive correlation with the degradation products of sulfated glycosaminoglycans. Our results suggest that in RA and ReA patients increased activity of GR does not prevent the increased degradation of collagen and proteoglycans by ROS.
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.