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Spectroscopic properties of fluorescently labelled mRNA cap analogues

100%

Szabelski M. , Ziemniak M. , Jemielity J. , Wieczorek Z.

2013

tom 36

nr 2A: Plenary lectures

Influence of organic solvents on papain kinetics

100%

Szabelski M. , Stachowiak K. , Wiczk W.

Acta Biochimica Polonica

2001

tom 48

nr 4

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.

Influence on Me2SO and incubation time on papain activity studied using fluorogenic substrates

100%

Szabelski M. , Stachowiak K. , Wiczk W.

Acta Biochimica Polonica

2001

tom 48

nr 4

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 Michae- lis-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.