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1

Episjalina - nowopoznany skladnik glikokaliksu i blony komorkowej komorek nablonkowych

100%
Gindzienski A., Zwierz K.
Postępy Biochemii
|
1997
|
tom 43
|
nr 2
80-84
2

Mucyna MUC1 i jej znaczenie w procesach nowotworzenia

100%
Paszkiewicz-Gadek A., Gindzienski A.
Postępy Biochemii
|
2000
|
tom 46
|
nr 4
342-350
3

Śluz i mucyna - problem biochemiczny i medyczny

100%
Gindzienski A., Zwierz K.
Postępy Biochemii
|
1991
|
tom 37
|
nr 3-4
4

Low molecular mass products of depolymerization of purified mucin - attempts at isolation and characterization

100%
Minkiewicz I., Gindzienski A.
Acta Biochimica Polonica
|
1999
|
tom 46
|
nr 4
Samples of crude mucin were incubated at room temperature for 48 and 96 h in a sodium azide containing buffer, pH 7.0. Then each sample was purified, reduced and alkylated with iodo[14C]acetamide. Electrophoretic analysis demonstrated that radioactivity was incorporated into the mucin subunits and proteins of 100 and 140 kDa. The results of our experiments suggest that the released proteins can be a part of mucin molecule, cleaved by proteolysis and reduction of disulfide bridges.
5

Isolation, purification and chemical composition of insoluble collagen from guerin epithelioma

81%
Bankowski E., Galasinski W., Gindzienski A., Rzeczycki W.
Acta Biochimica Polonica
|
1975
|
tom 22
|
nr 3
6
Content available remote

The role of mucus and its components in protection and repair within the alimentary tract mucosa: Polish experience

81%
Gindzienski A., Zwierz K., Sarosiek J.
Journal of Physiology and Pharmacology. Supplement
|
2003
|
tom 54
|
nr 3
127-144
The Gastroenterology Research Laboratory at New York Medical College, New York City, NY, directed by Prof. Dr. George B. Jerzy Glass and after his retirement by Prof. Dr. Bronislaw L. Slomiany and Prof. Dr. Amalia Slomiany served as a lunching pad for successful careers in exploration of mucus for Dr. Andrzej Gindzienski and Dr. Krzysztof Zwierz and Janusz Badurski at the Medical School in Bialystok, Poland as well as Dr. Jerzy Sarosiek at Gastroenterology Research Laboratory, University of Virginia Health Sciences Center, Charlottesville, VA and currently, Gastroenterology Research Laboratory, Kansas University Medical Center, Kansas City, KS, USA. The dynamic and insightful research endeavors implemented at the Medical School of Bialystok revealed new information regarding enzymatic pathways of mucin synthesis especially its carbohydrate components such as hexosamines. These discoveries become instrumental in our understanding of the alimentary tract mucin synthesis and function in health and disease. Similarly innovative mucus research conducted across the Atlantic Ocean uncovered the novelty of mucin elaborated within the esophageal submucosal mucous glands in humans by demonstration that its chemical characteristics are different both from human salivary and gastric mucins. In addition, a novel method for the measurement of the thickness of the gastric mucus layer ex vivo in humans has also been developed. These pioneering works are continued at both mucus exploration centers attracting younger generation of investigators enticed by the mystery of the structure and function of the mucus barrier and its leading role in mucosal protection against injury as well as immediate and unequivocal contribution to mucosal repair and reconstitution process.
7

N-acetylo-beta-D-heksozoaminidaza - enzym chorob Tay-Sachsa i Sandhoffa

81%
Zwierz K., Juszkiewicz J., Arciuch L., Gindzienski A.
Postępy Biochemii
|
1992
|
tom 38
|
nr 3
127-132
8

Glutahione reductase activity in synovial fluid from patients with reactive arthritis, osteoarthritis and rheumatoid arthritis

81%
Sredzinska K., Galicka A., Popko J., Gindzienski A.
Acta Biochimica Polonica
|
2006
|
tom 53
|
nr Supplement 1
9

Effect of cadmium on collagen content and solubility in rat bone

81%
Galicka A., Brzoska M. M., Sredzinska K., Gindzienski A.
Acta Biochimica Polonica
|
2004
|
tom 51
|
nr 3
The toxic action of cadmium in the bone tissue is known, but its mechanisms are still unexplained. We examined whether Cd influences collagen content and its solu­bility in the femoral bone of three-week-old female rats exposed to 5 or 50 mg Cd/l in drinking water. Non-cross linked collagen was extracted with 0.5 M acetic acid, and two acid-insoluble collagen fractions were extracted with pepsin and 4.0 M guanidine hydrochloride, respectively. SDS/PAGE showed the presence of two colla­gen types, I and V, in all three extracted fractions. Exposure of rats to Cd for 6 months increased the amount of acid-soluble collagens type I and V and decreased the level of acid-insoluble collagens. The amount of total collagen extracted from the bones of rats exposed to 50 mg Cd/l was reduced by about 14% as compared to con­trol and those intoxicated with 5 mg Cd/l. The solubility of type I bone collagen (de­termined as the percentage of acetic-soluble fraction of total collagen) was increased 2.9- and 3.0-fold in rats intoxicated with 5 and 50 mg Cd/l, respectively. Similarly, the solubility of type V collagen was increased 2.3- and 2.7-fold, respectively. Our re­sults indicate that Cd treatment affects bone collagen by decreasing its content and increasing its solubility.
10

EF-1alpha is a target site for inhibitory effect of quercetin in the peptide elongation process

81%
Marcinkiewicz C., Galasinski W., Gindzienski A.
Acta Biochimica Polonica
|
1995
|
tom 42
|
nr 3
The effect of quercetin (3,3',4',5,7-pentahydroxyflavone) on the polypeptide elon­gation system isolated from rat liver cells, was investigated. Quercetin inhibited [ 4C]leucine incorporation into proteins in vitro and the inhibitory effect is being directed towards the elongation factor eEF-1, but not to eEF-2 and ribosomes. Quer­cetin was found to form a complex with EF-la, which was inactive in GTP-dependent binding to ribosomes. It can be suggested that quercetin can block the total or the part of the domain of EF-la structure that is responsible for formation of the ternary complex EF-la-GTP-i14C]Phe-tRNA and therefore preventing formation of the quater­nary complex with ribosomes.
11

Application of aqueous hydrazine solution for beta-elimination of O-glycans from gastric mucin

81%
Kisiel D., Gindzienski A., Gadek A.
Acta Biochimica Polonica
|
1999
|
tom 46
|
nr 3
O-Glycans from pig gastric mucin were released by β-elimination in 0.2 M triethylamine and 50% aqueous hydrazine water solution. The released glycan hydrazides were isolated using Centricon 10 separators, brought to their reducing form and reductive by labelled with p-aminobenzoic acid ethyl ester (ABEE). Labelled products were fractionated into neutral and acid fractions on a Bio-Gel P4 column, calibrated with a mixture of dextran oligosaccharides, labelled according to the same procedure.
12

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

81%
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.
13

Purification and characterization of the protein kinase eEF-2 isolated from rat liver cells

81%
Gajko A., Galasinski W., Gindzienski A.
Acta Biochimica Polonica
|
1994
|
tom 41
|
nr 4
The elongation factor 2 (eEF-2) protein kinase was isolated from rat liver cells, purified and partly characterized. It was found that the enzyme exists in an inactive form in the homogenate of rat liver. The active fraction of kinase eEF-2 was obtained after removal of the inhibitory substance by hydroxyapatite column chromatography. The purified enzyme is an electTophoretically homogeneous protein with relative molecular mass of approximately 90000 and isoelectric point, pi = 5.9. The enzyme specifically phosphorylates the elongation factor eEF-2 in the presence of calmodulin and Ca2+.
14

Structure and biosynthesis of human salivary mucins

81%
Zalewska A., Zwierz K., Zolkowski K., Gindzienski A.
Acta Biochimica Polonica
|
2000
|
tom 47
|
nr 4
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.
15

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

81%
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.
16

Studies on type I collagen in skin fibroblasts cultured from twins with lethal osteogenesis imperfecta

81%
Galicka A., Wolczynski S., Gindzienski A.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr 2
Studies on type I procollagen produced by skin fibroblasts cultured from twins with lethal type II of osteogenesis imperfecta (OI) showed that biosynthesis of collagen (measured by l-[5- 3H]proline incorporation into proteins susceptible to the action of bacterial collagenase) was slightly increased as compared to the control healthy in­fant. SDS/PAGE showed that the fibroblasts synthesized and secreted only normal type I procollagen. Electrophoretic analysis of collagen chains and CNBr peptides showed the same pattern of electrophoretic migration as in the controls. The lack of posttranslational overmodification of the collagen molecule suggested a molecular de­fect near the amino terminus of the collagen helix. Digestion of OI type I collagen with trypsin at 30°C for 5 min generated a shorter than normal a2 chain which melted at 36°C. Direct sequencing of an asymmetric PCR product revealed a heterozygous sin­gle nucleotide change C->G causing a substitution of histidine by aspartic acid in the a2 chain at position 92. Pericellular processing of type I procollagen by the twin's fibroblasts yielded a later appearance of the intermediate pC-ai(I) form as compared with control cells.
17

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
18

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
19

A novel Gly to Arg substitution at position 388 of the alpha1 chain of type I collagen in lethal form of osteogenesis imperfecta

71%
Galicka A., Wolczynski S., Lesniewicz R., Chyczewski L., Gindzienski A.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 2
Cultured skin fibroblasts from a proband with a lethal form of osteogenesis imperfecta produce two forms of type I collagen chains, with normal and delayed elec- trophoretic migration; collagen of the proband's mother was normal. Peptide map­ping experiments localized the structural defect in the proband to a 1(I) CB8 peptide in which residues 123 to 402 are spaned. Direct sequencing of amplified cDNA covering this region revealed a G to A single base change in one allele of the al(I) chain, that converted glycine 388 to arginine. Restriction enzyme digestion of the RT-PCR prod­uct was consistent with a heterozygous COL1A1 mutation. The novel mutation con­forms to the linear gradient of clinical severity for the αl(I) chain and results in re­duced thermal stability by 3°C and intracellular retention of abnormal molecules.
20

Isolation of MUC1 mucin from human ascitic fluid by affinity chromatography method

61%
Radziejewska I., Kisiel D. G., Borzym-Kluczyk M., Kluz A., Wosek J., Gindzienski A.
Acta Biochimica Polonica
|
2006
|
tom 53
|
nr Supplement 1
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