Temat: fluorogenic substrate - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: Optimization of measurement enzyme activity using fluorogenic substrates in water
Optymalizacja pomiaru enzymatycznej aktywności w wodzie z użyciem substratów fluorogennych
Autorzy:: Skorczewski, P.
Mudryk, Z.
Kulinski, B.
Powiązania:: https://bibliotekanauki.pl/articles/85155.pdf
Data publikacji:: 1999
Wydawca:: Akademia Pomorska w Słupsku
Tematy:: measurement
enzyme activity
fluorogenic substrate
water
temperature
pH
mercuric chloride
brackish water
organic matter
dissolved organic matter
particulate organic matter
aquatic ecosystem
Lake Gardno
Źródło:: Baltic Coastal Zone. Journal of Ecology and Protection of the Coastline; 1999, 03
1643-0115
Pojawia się w:: Baltic Coastal Zone. Journal of Ecology and Protection of the Coastline
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 2.

Tytuł:: Fluorogenic peptide substrates for carboxydipeptidase activity of cathepsin B.
Autorzy:: Stachowiak, Krystyna
Tokmina, Monika
Karpińska, Anna
Sosnowska, Renata
Wiczk, Wiesław
Powiązania:: https://bibliotekanauki.pl/articles/1043322.pdf
Data publikacji:: 2004
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: fluorogenic substrate
cathepsin B
cystatins
Opis:: Cathepsin B is a lysosomal cysteine protease exhibiting mainly dipeptidyl carboxypeptidase activity, which decreases dramatically above pH 5.5, when the enzyme starts acting as an endopeptidase. Since the common cathepsin B assays are performed at pH 6 and do not distinguish between these activities, we synthesized a series of peptide substrates specifically designed for the carboxydipeptidase activity of cathepsin B. The amino-acid sequences of the P5-P1 part of these substrates were based on the binding fragments of cystatin C and cystatin SA, the natural reversible inhibitors of papain-like cysteine protease. The sequences of the P'1-P'2 dipeptide fragments of the substrates were chosen on the basis of the specificity of the S'1-S'2 sites of the cathepsin B catalytic cleft. The rates of hydrolysis by cathepsin B and papain, the archetypal cysteine protease, were monitored by a continuous fluorescence assay based on internal resonance energy transfer from an Edans to a Dabcyl group. The fluorescence energy donor and acceptor were attached to the C- and the N-terminal amino-acid residues, respectively. The kinetics of hydrolysis followed the Michaelis-Menten model. Out of all the examined peptides Dabcyl-R-L-V-G-F- E(Edans) turned out to be a very good substrate for both papain and cathepsin B at both pH 6 and pH 5. The replacement of Glu by Asp turned this peptide into an exclusive substrate for cathepsin B not hydrolyzed by papain. The substitution of Phe by Nal in the original substrate caused an increase of the specificity constant for cathepsin B at pH 5, and a significant decrease at pH 6. The results of kinetic studies also suggest that Arg in position P4 is not important for the exopeptidase activity of cathepsin B, and that introducing Glu in place of Val in position P2 causes an increase of the substrate preference towards this activity.
Źródło:: Acta Biochimica Polonica; 2004, 51, 1; 81-92
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 3.

Tytuł:: Influence of Me2SO and incubation time on papain activity studied using fluorogenic substrates.
Autorzy:: Szabelski, Mariusz
Stachowiak, Krystyna
Wiczk, Wiesław
Powiązania:: https://bibliotekanauki.pl/articles/1044042.pdf
Data publikacji:: 2001
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: fluorogenic substrate
enzyme activity
papain
Me2SO
Opis:: Papain activity in a buffer containing Me2SO was studied using fluorogenic substrates. It was found that the number of active sites of papain decreases with increasing Me2SO concentration whereas the incubation time, in a buffer containing 3% Me2SO does not affect the number of active sites. However, an increase of papain incubation time in the buffer with 3% Me2SO decreased the initial rate of hydrolysis of Z-Phe-Arg-Amc as well as Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans. Moreover, an increase of Me2SO concentration in working buffer decreased the initial rate of papain-catalysed hydrolysis of both substrates. A rapid decrease of the initial rate (by up to 30%) was observed between 1 and 2% Me2SO. Application of the Michaelis-Menten equation revealed that at the higher Me2SO concentrations the apparent values of kcat/Km decreased as a result of Km increase and kcat decrease. However, Me2SO changed the substrate binding process more effectively (Km) than the rate of catalysis kcat..
Źródło:: Acta Biochimica Polonica; 2001, 48, 4; 995-1002
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 4.

Tytuł:: Influence of organic solvents on papain kinetics
Autorzy:: Szabelski, Mariusz
Stachowiak, Krystyna
Wiczk, Wiesław
Powiązania:: https://bibliotekanauki.pl/articles/1044084.pdf
Data publikacji:: 2001
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: organic solvent
fluorogenic substrate
enzyme activity
papain
Opis:: Papain activity was studied in water-organic solvent mixtures using the fluorogenic substrate Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans. The increase of organic solvent (MeOH, EtOH, iPrOH, TFE, MeCN, (MeO)2Et and DMF) concentration in the mixture caused a substantial decrease the initial rate of papain-catalyzed hydrolysis. Moreover, the number of papain active sites decreased with the increase of DMF and MeOH concentration.
Źródło:: Acta Biochimica Polonica; 2001, 48, 4; 1197-1201
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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