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1
Białkowe aktywatory biosyntezy i metabolizmu cholesterolu
100%
Wojciechowski Z. A.
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nr 1-2
2
Intracellular localization and some properties of UDPG: sterol glucosyltransferase from Calendula officinalis
63%
Wojciechowski Z. A. , Van Uon N.
Acta Biochimica Polonica
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1975
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tom 22
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nr 1
3
TLC and GLC analysis of individual molecular species in natural mixtures of steryl glycosides isolated from eggplant
63%
Zimowski J. , Wojciechowski Z. A.
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1996
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tom 42
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nr 4
269-272
PL
Opracowano prostą, dwustopniową metodę analizy składu naturalnych frakcji roślinnych glikozydów steroli. Metoda polega na wstępnym rozdzieleniu frakcji, ze względu na rodzaj składnika cukrowego, metodą chromatografii cienkowarstwowej i następnym rozdzieleniu poszczególnych glikozydów, ze względu na rodzaj składnika sterolowego, metodą chromatografii gazowej.
EN
A simple, two-step method for analysis of plant steryl glycosides is described. In the first step steryl glycosides are separated by TLC according to their sugar component. In the second step steryl glycosides are separated by GLC according to their sterol component.
4
The in vitro synthesis of diosgenin mono- and diglucoside by enzyme preparations from Solanum melongena leaves
63%
Paczkowski C. , Wojciechowski Z. A.
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1993
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tom 40
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nr 1
5
Biosynthesis and metabolism of cucurbitacins and sterols at early stages of development of Cucumis sativus L plants
51%
Kintia P. K. , Wojciechowski Z. A. , Kasprzyk Z.
Acta Biochimica Polonica
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1974
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tom 21
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nr 3
6
Characterization of acyllipid:sterol glucoside acyltransferase from oat (Avena Sativa L.) seedlings
51%
Misiak M. , Kalinowska M. , Wojciechowski Z. A.
Acta Biochimica Polonica
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1991
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tom 38
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nr 1
7
UDP-glucose: solasodine glucosyltransferase from eggplant [Solanum melongena L.] leaves: Partial purification and characterization
51%
Paczkowski C. , Kalinowska M. , Wojciechowski Z. A.
Acta Biochimica Polonica
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1997
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tom 44
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nr 1
EN
Uridine 5 '-diphosphoglucose-dependent glucosyltransferase which catalyzes the glucosylation of solasodine, i.e. UDP-glucose:solasodine glucosyltrans­ferase, is present in leaves, roots, unripe fruits and unripe seeds of eggplant (Solanum melongenaL.). The glucosylation product is chromatographically identical with authentic solasodine 3β-nmonoglucoside, a putative intermedi­ate in the biosynthesis of solasodine-based glycoalkaloids characteristic of the eggplant. The enzyme was purified about 50-fold from crude cytosol fraction of eggplant leaves by ammonium sulphate precipitation and column chromatog­raphy on Q-Sepharose and Sephadex G-100. The native enzyme has a molecular mass of approx. 55 and pH optimum of 8.5. metal ions are not required for its activity but the presence of free -SH groups is essential. Besides solasodine (Km = 0.04 ), the enzyme effectively glucosylates tomatidine, another steroidal alkaloid of the spirosolane type, but it is virtually inactive towards the solanidane-type steroidal alkaloids such as solanidine or demissid- ine. The enzyme is specific for UDP-glucose (Km= 2.1 u) since unlabelled ADP-, GDP-, CDP- or TDP-glucose could not effectively compete with UDP-[14]glucose used as the sugar donor for solasodine glucosylation. Moreover, no synthe­sis of labelled solasodine galactoside was observed when UDP-l14]glucose was replaced with UDP-[l4]galactose.
8
Evidence for essential histidine and dicarboxylic amino-acid residues in the active site of UDP-glucose: solasodine glucosyltransferase from eggplant leaves
51%
Nawloka P. , Kalinowska M. , Paczkowski C. , Wojciechowski Z. A.
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nr 2
EN
Effects of several chemical probes selectively modifying various amino-acid resi­dues on the activity of UDP-glucose : solasodine glucosyltransferase from eggplant leaves was studied. It was shown that diethylpyrocarbonate (DEPC), a specific modi­fier of histidine residues, was strongly inhibitory. However, in the presence of exces­sive amounts of the enzyme substrates, i.e. either UDP-glucose or solasodine, the in­hibitory effect of DEPC was much weaker indicating that histidine (or histidines) are present in the active site of the enzyme. Our results suggest also that unmodified resi­dues of glutamic (or aspartic) acid, lysine, cysteine, tyrosine and tryptophan are nec­essary for full activity of the enzyme. Reagents modifying serine and arginine resi­dues have no effect on the enzyme activity.
9
Słownictwo. II. Słownictwo retinoidów
26%
Wojciechowski Z. A.
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nr 1-2
10
Słownictwo. I. Słownictwo prenoli
26%
Wojciechowski Z. A.
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nr 1-2
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