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Wyświetlanie 1-10 z 10
Tytuł:
Low molecular mass products of depolymerization of purified mucin - attempts at isolation and characterization
Autorzy:
Minkiewicz, Iwona
Gindzieński, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1044451.pdf
Data publikacji:
1999
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
disulfide bridges
subunits
isolation
mucin
Opis:
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.
Źródło:
Acta Biochimica Polonica; 1999, 46, 4; 928-933
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Studies on type I collagen in skin fibroblasts cultured from twins with lethal osteogenesis imperfecta.
Autorzy:
Galicka, Anna
Wołczyński, Sławomir
Gindzieński, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1043625.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
osteogenesis imperfecta
type I collagen
Opis:
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 α2 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 α2 chain at position 92. Pericellular processing of type I procollagen by the twin's fibroblasts yielded a later appearance of the intermediate pC-α1(I) form as compared with control cells.
Źródło:
Acta Biochimica Polonica; 2003, 50, 2; 481-488
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
EF-1α Is a target site for an inhibitory effect of quercetin in the peptide elongation process
Autorzy:
Marcinkiewicz, Cezary
Gałasiński, Władysław
Gindzieński, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1045226.pdf
Data publikacji:
1995
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1995, 42, 3; 347-350
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The participation of ribosome-UDP-GalNAc complex in the initiation of protein glycosylation in vitro
Autorzy:
Paszkiewicz-Gadek, Anna
Porowska, Halina
Gindzieński, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1044369.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
glycosylation
UDP-GalNAc-transferase
UDP-GalNAc
apomucin
ribosome
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2000, 47, 2; 421-426
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Activity of partially purified UDP-N-acetyl-α-D-galacto- samine:polypeptide N-acetylgalactosaminyltransferase with different peptide acceptors
Autorzy:
Porowska, Halina
Paszkiewicz-Gadek, Anna
Gindzieński, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1044518.pdf
Data publikacji:
1999
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1999, 46, 2; 365-370
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Effect of cadmium on collagen content and solubility in rat bone.
Autorzy:
Galicka, Anna
Brzóska, Małgorzata
Średzińska, Krystyna
Gindzienski, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1041563.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
rat
collagen
bone
cadmium
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2004, 51, 3; 825-829
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
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:
A novel Gly to Arg substitution at position 388 of the α1 chain of type I collagen in lethal form of osteogenesis imperfecta.
Autorzy:
Galicka, Anna
Wolczynski, Slawomir
Lesniewicz, Ryszard
Chyczewski, Lech
Gindzienski, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1043783.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
osteogenesis imperfecta
collagen
Opis:
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 electrophoretic migration; collagen of the proband's mother was normal. Peptide mapping experiments localized the structural defect in the proband to α1(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 α1(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 α1(I) chain and results in reduced thermal stability by 3°C and intracellular retention of abnormal molecules.
Źródło:
Acta Biochimica Polonica; 2002, 49, 2; 443-450
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-10 z 10

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