Prispevek predstavlja ugotovitve raziskave, ki se je osredotočala na vlogo mentorja pri umetniškem ustvarjanju v skupini odraslih z motnjo v duševnem razvoju. Podatki so bili zbrani v obdobju ...2014–2016 z metodo opazovanja z udeležbo ter s pomočjo polstrukturiranih intervjujev z mentorji. Raziskava izhaja iz predpostavke, da je umetniško ustvarjanje pomemben del življenja in izobraževanja oseb z motnjo v duševnem razvoju. Vloga mentorja, ki vodi skupino oseb z motnjo v duševnem razvoju, se razlikuje od vloge mentorja v skupinah oseb brez motnje v duševnem razvoju. Rezultati raziskave so predstavljeni po sklopih, ki zajemajo ugotovitve o izbranih področjih delovanja mentorja: motiviranje skupine, vodenje, spodbujanje samostojnosti udeležencev, individualizacija in prilagajanje procesa udeležencem, prilagajanje aktivnosti dejanski starosti oseb z motnjo v duševnem razvoju, vključevanje udeležencev v nastajanje procesa, kombiniranje različnih aktivnosti.
This thesis describes the ionic strength and ion binding effects on the oxidation reduction properties of cytochrome c and its lysine modified derivatives.
Cytochrome c has been modified in two ...different ways: a complete modification of all lysine residues and specific modification of one lysine residue. Some properties of the modified derivatives are described.
Ion binding properties of cytochrome c and its lysine modified derivatives were studied by measuring the apparent equilibrium constant of the reaction between the;
ferri- form of the protein and potassium ferrocyanide. It was found that unmodified cytochrome c binds one cation (K+, Na+) per molecule, and binding is much stronger to the reduced form of the protein. Binding of cations is not changed upon modification of the lysine residues. For binding of the chloride, there are two binding sites on the cytochrome c molecule, and the binding is much stronger to the oxidized form of the protein. It was shown that upon the modification of the lysine residues in either way the binding of chloride was considerably changed. It was concluded that one of these two binding sites for chloride on cytochrome c involves lysine residue, probably the residue number 13.
Thesis
Master of Science (MSc)
The biosynthesis of the Lewis X determinant (Gal beta 1-4 Fuc alpha 1-3GlcNAc beta-) in three strains of Helicobacter pylori has been investigated. Strains UA 861, UA 802 and UA 1182 contain alpha ...1,3 fucosyltransferase and beta 1,4 galactosyltransferase activities that synthesize the Lewis X structure by the transfer of monosaccharides from GDP-fucose and UDP-galactose donors, respectively. The enzyme reaction products that formed were characterized by capillary zone electrophoresis and by 1H-NMR spectroscopy. The biosynthetic pathway is therefore identical to that found in humans. In the three strains, the fucosyltransferase and galactosyltransferase activities differed in various cellular fractions. Km values for their donor and acceptor substrates also differed.
The Lewis (α 1–3/4) fucosyltransferase isolated from human milk could be used for preparative fucosylations of the disaccharide acceptors Gal(β 1–3)GlcNAc(β 1-O)R (at position OH-4) and Gal(β ...1–4)GlcNAc(β 1-O)R (at position OH-3)
R = (
CH
2)
8
COOMe. As donors GDP-
l-Gal and deoxygenated derivatives were used to lead to a series of novel modified trisaccharides of the Lewis
a and the Lewis
x type, respectively.
The branching enzyme
N-acetylglucosaminyltransferase-V (GlcNAcT-V) recognizes the trisaccharide
β-
d-Glc
p
NAc-(1 → 2)-α-
d-Man
p-(1 → 6)-β-
d-Glc
p-
O(CH
2)
7CH
3
(1) as its minimum substrate. We ...report here the chemical synthesis of
β-
d-Glc
p
NAc-(1 → 2)-
5a-carba-α-
d-Man
p-(1 → 6)-β-
d-Glc
p-
O(CH
2)
7CH
3
(2), a carbocyclic analog of
1 where the ring oxygen of the
α-
d-Man
p
residue is replaced by a methylene group. Trisaccharide
2 was found to be fully active as an acceptor for GlcNAcT-V, both with the enzyme isolated from hamster kidney and the one cloned from rat kidney. The kinetic parameters
K
m and
V
max for 1 and 2 were functionally equivalent. A preparative glycosylation reaction was performed using 2 as the acceptor with the cloned rat kidney enzyme. A tetrasaccharide formed by the addition of a Glc
pNAc residue was the sole product as detected by
1H NMR spectroscopy and FAB mass spectrometry and was assigned the structure
β-
d-Glc
p
NAc-(1 → 2)-β-
d-Glc
p
NAc-(1 → 6)-
5a-carba-α-
d-Man
p-(1 → 6)-β-
d-Glc
p-
O(CH
2)
7CH
3
(13).
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