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1

Podejście instytucjonalne w geografii ekonomicznej i badaniach regionalnych

100%
Stachowiak K.
Biuletyn PAN. Komitet Przestrzennego Zagospodarowania Kraju
|
2008
|
nr 237
2

Institutional approach in economic geography and its relevance to regional studies

63%
Stachowiak K., Stryjakiewicz T.
Quaestiones Geographicae
|
2008
|
tom 27B
|
nr 1
3

Ocena biologicznej wartosci pokarmowej mieszanek paszowych z udzialem roznych premiksow w zywieniu kur niesnych

63%
Gornowicz E., Stachowiak K.
Postępy Drobiarstwa
|
1996
|
tom 34
|
nr 4
12-18
4

Sojax w zywieniu kurczat brojlerow

63%
Gornowicz E., Stachowiak K.
Postępy Drobiarstwa
|
1996
|
tom 34
|
nr 3
17-24
5

'Folwark Mila'

63%
Zielinska K., Stachowiak K.
Poradnik Gospodarski
|
2008
|
nr 11
47
6

Zastosowanie kwasu mlekowego w odchowie kurczat brojlerow

63%
Gornowicz E., Stachowiak K.
Postępy Drobiarstwa
|
1996
|
tom 34
|
nr 1
5-10
7

Ocena biologicznej wartosci pokarmowej mieszanek dla kurczat brojlerow

63%
Stachowiak K., Gornowicz E.
Biuletyn Informacyjny Drobiarstwa
|
1992
|
tom 30
|
nr 5
10-12
8

Zywienie kogutow reprodukcyjnych typu miesnego

63%
Stachowiak K., Gornowicz E.
Postępy Drobiarstwa
|
1996
|
tom 34
|
nr 3
11-16
9

Konferencja naukowa „Nowe problemy badawcze geografii społecznoekonomicznej i gospodarki przestrzennej”, 11–12 czerwca 2018 r., Poznań.

63%
Stachowiak K., Dominiak J.
Przegląd Geograficzny. Polska Akademia Nauk
|
2018
|
tom 90
|
nr 4
10

Wplyw zywienia kurczat brojlerow na zawartosc amoniaku w kurniku

63%
Gornowicz E., Stachowiak K.
Postępy Drobiarstwa
|
1996
|
tom 34
|
nr 2
5-9
11

Location patterns and location factors in the cultural and creative industries

63%
Tomczak P., Stachowiak K.
Quaestiones Geographicae
|
2015
|
tom 34
|
nr 2
12

Dzień Otwartej Zagrody w powiecie leszczyńskim

63%
Stachowiak K.
Poradnik Gospodarski
|
2014
|
nr 07-08
13

Wielkopolskie Fora Rolnicze w powiecie leszczyńskim

63%
Stachowiak K.
Poradnik Gospodarski
|
2016
|
nr 03
14
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Zmiany w proporcjach ciała buhajków odchowanych w centralnych wychowalniach

51%
Grabowski R., Stachowiak K., Dymnicki E.
Zeszyty Problemowe Postępów Nauk Rolniczych
|
1985
|
tom 300
15

Role of creative industries in the post-socialist urban transformation

51%
Stryjakiewicz T., Meczynski M., Stachowiak K.
Quaestiones Geographicae
|
2014
|
tom 33
|
nr 2
16

Influence of organic solvents on papain kinetics

51%
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.
17

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

51%
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.
18

Fluorogenic peptide substrates for carboxydipeptidase activity of cathepsin B

45%
Stachowiak K., Tokmina M., Karpinska A., Sosnowska R., Wiczk W.
Acta Biochimica Polonica
|
2004
|
tom 51
|
nr 1
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-FE(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.
19

Effect of antisense peptide binding on the dimerization of human cystatin C - gel electrophoresis and molecular modeling studies

39%
Stachowiak K., Rodziewicz-Motowidlo S., Sosnowska R., Kasprzykowski F., Lankiewicz L., Grubb A., Grzonka Z.
Acta Biochimica Polonica
|
2004
|
tom 51
|
nr 1
Human cystatin C (HCC) shows a tendency to dimerize. This process is particularly easy in the case of the L68Q HCC mutant and might lead to formation of amyloid de­posits in brain arteries of young adults. Our purpose was to find ligands of monomeric HCC that can prevent its dimerization. Eleven antisense peptide ligands of monomeric HCC were designed and synthesized. The influence of these ligands on HCC dimerization was studied using gel electrophoresis and molecular modeling methods. The results suggest that all the designed peptides interact with monomeric HCC facilitating its dimerization rather than preventing it.
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