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1

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.
2

Theoretical studies of binding modes of two covalent inhibitors of cysteine proteases

86%
Drabik P., Politowska E., Czaplewski C., Kasprzykowski F., Lankiewicz L., Ciarkowski J.
Acta Biochimica Polonica
|
2000
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tom 47
|
nr 4
Physiological and pathological roles of cysteine proteases make them important targets for inhibitor development. Although highly potent inhibitors of this group of enzymes are known, their major drawback is a lack of sufficient specificity. Two cysteine protease covalent inhibitors, viz. (i) Z-RL-deoxo-V-peptide-epoxysuccinyl hybrid, and (ii) Z-RLVG-methyl-, have been developed and modeled in the catalytic pocket of papain, an archetypal thiol protease. A number of configurations have been generated and relaxed for each system using the AMBER force field. The catalytic pockets S3 and S4 appear rather elusive in view of the observed inhibitors' flexibility. This suggest rather limited chances for the development of selective structure-based inhibitors of thiol proteases, designed to exploit differences in the structure of catalytic pockets of various members of this family.
3

Effect of papain and piperonyl butoxide/MGK-264 on the reproduction/development of Lymnaea acuminata

72%
Hanif F., Singh D. K.
Journal of Biology and Earth Sciences
|
2013
|
tom 03
|
nr 1
4
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Influence of Anisakis simplex stage III larvae upon the activity of proteases under in vitro conditions

72%
Dziekonska-Rynko J., Rokicki J., Jablonowski Z.
Wiadomości Parazytologiczne
|
2002
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tom 48
|
nr 2
The larvae of Anisakis simplex had the largest influence upon decreasing the activity of porcine pepsin. The activity of that enzyme in tests, where the larvae were present during the entire period of incubation, was lower than in the controls. No similar trends were observed in case of the solutions with bovine and porcine trypsin. The activity of those enzymes in the solutions containing the larvae was higher than in the controls. Only the activity of porcine trypsin after 10 h of incubation was slightly lower in the experimental sample than in the control, however, during the later hours the dynamics of the activity decrease of that enzyme in the controls was higher than in the experimental samples. The recorded activity of papain in the samples containing the larvae was higher than that in the controls during the entire time of the experiment.
5

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

72%
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.
6

Crystallization and preliminary crystallographic studies of a new crystal form of papain from Carica papaya

72%
Kozak M., Kozian E., Grzonka Z., Jaskolski M.
Acta Biochimica Polonica
|
1997
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tom 44
|
nr 3
A new crystal form of papain from the latex of Carica papaya, complexed with an inhibitor (Z-Arg-Leu-Val-Gly-CHN2) was obtained by the vapor-diffusion method using a methanol/ethanol mixture as a precipitant. The slat-like crys­tals are monoclinic, space group P2 1, with unit cell parameters a = 42.6 A, b = 49.8 A, c = 50.5 A, β= 111.9°, and contain one molecule in the asymmetric unit. The crystals are stable in the X-ray beam and diffract beyond 1.8 A. A molecular model has been placed in the unit cell by molecular replacement.
7

The impact of animal and plant proteases on Nematoda 3rd stage Anisakis simples larvae

58%
Dziekonska-Rynko J., Rokicki J., Jablonowski Z.
Oceanological Studies
|
1997
|
tom 26
|
nr 1
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