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Wyszukujesz frazę "UDP" wg kryterium: Temat


Wyświetlanie 1-3 z 3
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:
Metabolism of conjugated sterols in eggplant. Part 1. UDP-glucose : sterol glucosyltransferase
Autorzy:
Potocka, Anna
Zimowski, Jan
Powiązania:
https://bibliotekanauki.pl/articles/1040826.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
plant sterols
UDP-glucose : sterol glucosyltransferase
Solanum melongena
steryl glucoside
Opis:
A membrane-bound UDP-glucose : sterol glucosyltransferase from Solanum melongena (eggplant) leaves was partially purified and its specificity as well as molecular and kinetic properties were defined. Among a wide spectrum of 3-OH steroids (i.e. typical plant sterols, androstane, pregnane and cholestane derivatives, steroidal alkaloids and sapogenins) and triterpenic alcohols, the highest activity was found with 22-oxycholesterol. UDP-glucose appeared to be the best sugar donor. The enzyme preparation was also able to utilize UDP-galactose, TDP-glucose and CDP-glucose as a sugar source for sterol glucosylation, however, at distinctly lower rates. The investigated glucosyltrasferase was stimulated by 2-mercaptoethanol, Triton X-100 and negatively charged phospholipids, and inhibited in the presence of UDP, mono-, di- and triacylglycerols, divalent cations such as Zn2+, Co2+, high ionic strength, cholesteryl glucoside, galactoside and xyloside and some amino acid-modifying reagents (SITS, DIDS, PLP, DEPC, pCMBS, NEM, WRK and HNB). Our results suggest that unmodified residues of lysine, tryptophan, cysteine, histidine and dicarboxylic amino acids are essential for full enzymatic activity and indicate that a glutamic (or aspartic) acid residue is necessary for the binding of sugar donor, i.e. UDP-glucose in the active site of the GT-ase while histidine and cysteine residues are both important for the binding of the nucleotide-sugar as well as of the steroidal aglycone.
Źródło:
Acta Biochimica Polonica; 2008, 55, 1; 127-134
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Molecular basis of cellulose biosynthesis disappearance in submerged culture of Acetobacter xylinum
Autorzy:
Krystynowicz, Alina
Koziołkiewicz, Maria
Wiktorowska-Jezierska, Agnieszka
Bielecki, Stanisław
Klemenska, Emilia
Masny, Aleksander
Płucienniczak, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1041378.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
2-D electrophoresis
UDP-glucose pyrophosphorylase
phosphoglucomutase
bacterial cellulose
Acetobacter xylinum
PCR-MP
Opis:
Acetobacter xylinum strains are known as very efficient producers of bacterial cellulose which, due to its unique properties, has great application potential. One of the most important problems faced during cellulose synthesis by these bacteria is generation of cellulose non-producing cells, which can appear under submerged culture conditions. The reasons of this remain unknow. These studies have been undertaken to compare at the molecular level wild-type, cellulose producing (Cel+) A. xylinum strains with Cel- forms of cellulose-negative phenotype. Comparison of protein profiles of both forms of A. xylinum by 2D electrophoresis allowed for the isolation of proteins which were produced exclusively by either Cel+ or Cel- cells. Sequences of peptides derived from these proteins were aligned with those of proteins deposited in databases. This analysis revealed that Cel- cells lacked two enzymes: phosphoglucomutase and glucose-1-phosphate uridylyltransferase, which generates UDP-glucose being the substrate for cellulose synthase. DNA was analyzed by ligation-mediated PCR carried out at low denaturation temperature (PCR-MP). Two DNA fragments of different thermal stability (218 and 217 bp) were obtained from the DNA of Cel+ and Cel- forms, respectively. The only difference between these Cel- and Cel+ DNA fragments is deletion of one T residue. Alignment of those two sequences with those deposited in the GenBank database revealed that similar fragments are present in the genomes of some bacterial cellulose producers and are located downstream from open reading frames (ORF) encoding phosphoglucomutase. The meaning of this observation is discussed.
Źródło:
Acta Biochimica Polonica; 2005, 52, 3; 691-698
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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