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Effect of tartaric acid on conformation and stability of human prostatic phosphatase: An infrared spectroscopic and calorimetric study.

100%

Bem S., Ostrowski W. S.

2001

vol. 48

issue 3

755-762

The solution structure and thermal stability of human prostatic acid phosphatase (hPAP) in the absence and in the presence of tartaric acid were studied by Fourier transform infrared spectroscopy (FTIR) and differential scanning calorimetry (DSC). The temperature dependence of the infrared spectrum and DSC scans indicate that hPAP undergoes thermal unfolding at a temperature between 49.5 and 52.5°C. Binding of tartaric acid does not lead to major changes in the secondary structure of hPAP, however, hPAP with bound tartaric acid shows a significantly increased thermal stability. These results helped to better understand the mechanism of hPAP unfolding at the elevated temperature.

The 35 kDa acid metallophosphatase of the frog Rana esculenta liver: studies on its cellular localization and protein phosphatase activity.

88%

Szalewicz A., Strzelczyk B., Sopel M., Kubicz A.

2003

vol. 50

issue 2

555-566

The cellular localization of the 35 kDa, low molecular mass acid metallophosphatase (LMW AcPase) from the frog (Rana esculenta) liver and its activity towards P-Ser and P-Tyr phosphorylated peptides were studied. This enzyme was localized to the cytoplasm of hepatocytes but did not appear in other cells of liver tissue (endothelium, macrophages, blood cells). This LMW AcPase does not display activity towards 32P-phosphorylase a under conditions standard for the enzymes of PPP family. Proteins containing P-Ser: rabbit 32P-phosphorylase a and phosvitin are hydrolysed only at acidic pH and are poor substrates for this enzyme. The frog AcPase is not inhibited by okadaic acid and F- ions, the Ser/Thr protein phosphatase inhibitors. Moreover, the frog enzyme does not cross-react with specific antisera directed against N-terminal fragment of human PP2A and C-terminal conserved fragment of the eukaryotic PP2A catalytic subunits. These results exclude LMW AcPase from belonging to Ser/Thr protein phosphatases: PP1c or PP2Ac. In addition to P-Tyr, this enzyme hydrolyses efficiently at acidic pH P-Tyr phosphorylated peptides (hirudin and gastrin fragments). Km value for the hirudin fragment (7.55 ± 1.59 × 10-6 M) is 2-3 orders of magnitude lower in comparison with other substrates tested. The enzyme is inhibited competitively by typical inhibitors of protein tyrosine phosphatases (PTPases): sodium orthovanadate, molybdate and tungstate. These results may suggest that the LMW AcPase of frog liver can act as PTPase in vivo. A different cellular localization and different response to inhibition by tetrahedral oxyanions (molybdate, vanadate and tungstate) provide further evidence that LMW AcPase of frog liver is distinct from the mammalian tartrate-resistant acid phosphatases.

Wpływ kąpieli w zimnej wodzie na powysiłkową aktywność a1-antytrypsyny i wybranych enzymów lizosomalnych we krwi zdrowych mężczyzn – doniesienia wstępne

63%

Pawłowska M., Mila- Kierzenkowska C., Boraczyński T., Boraczyński M., Sutkowy P., Paprocki J., Woźniak A.

Polish Journal of Sports Medicine

2017

vol. 33(3)

193-201

Background. The aim of the study was to determine the effect of winter bath after physical exercise on the activity of α1-antitrypsin (AAT) and selected lysosomal enzymes: arylsulfatase (ASA), acid phosphatase (AcP) and cathepsin D (CTS D) in healthy males’ blood. Material and methods. 22 males participated in two session of aerobic physical exercise. After one session the subjects rested in room temperature while after the other session they bathed in cold water (3 minutes, 8ºC; experiment 2). During each stage they had blood taken from the basilic vein prior to physical exercise and 2 and 20 minutes after the exercise. The activity of AAT, ASA, AcP and CTS D was assayed in blood serum. The obtained results were subjected to statistical analysis using ANOVA test. The changes at the level p<0.05 were regarded as statistically significant. Results. A statistically significant increase in AcP and CTS D activity was found as well as a decrease in AAT activity following physical exercise and resting at room temperature as compared with the activity of the assayed parameters prior to physical exercise. Conversely, no statistically significant differences in protease inhibitor activity (AAT) and lysosomal enzyme activity were noted after physical exercise and cold water bath as compared with their activity measured prior to 30-minute long physical exercise. Conclusions. Hot water bath applied after physical exercise increases the stability of lysosomal membranes and may result in a decrease of post-exercise muscle damage.

Wstęp. Celem pracy było określenie wpływu kąpieli w zimnej wodzie zastosowanej po wysiłku fizycznym na aktywność α1-antytrypsyny (AAT) oraz wybranych enzymów lizosomalnych: arylosulfatazy (ASA), kwaśnej fosfatazy (AcP) i katepsyny D (CTS D) we krwi zdrowych mężczyzn. Materiał i metody. 22 mężczyzn poddano dwóm sesjom 30-min. aerobowego wysiłku fizycznego. Po jednym z nich mężczyźni odpoczywali w temperaturze pokojowej, podczas gdy po drugim poddano ich kąpieli w zimnej wodzie (3 min, 8ºC; doświadczenie 2). W każdym z etapów krew pobrano trzykrotnie z żyły odłokciowej: przed wysiłkiem fizycznym oraz 2 i 20 min. po zakończeniu wysiłku. W surowicy krwi oznaczono aktywności AAT, ASA, AcP i CTS D. Uzyskane wyniki poddano analizie statystycznej za pomocą testu ANOVA. Zmiany na poziomie p<0,05 uznano za istotne statystycznie. Wyniki. Wykazano istotny statystycznie wzrost aktywności AcP i CTS D oraz obniżenie aktywności AAT po wysiłku fizycznym i odpoczynku w temperaturze pokojowej w porównaniu do aktywności oznaczanych parametrów przed wysiłkiem fizycznym. Nie odnotowano natomiast istotnych statystycznie różnic aktywności inhibitora proteaz (AAT) oraz oznaczanych enzymów lizosomalnych po wysiłku fizycznym i kąpieli w zimnej wodzie w porównaniu z ich aktywnością przed 30-minutowym wysiłkiem. Wnioski. Kąpiel w zimnej wodzie zastosowana po wysiłku fizycznym zwiększa stabilność błon lizosomalnych i może skutkować zmniejszeniem powysiłkowych uszkodzeń mięśni.

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2 Acta Biochimica Polonica

1 Polish Journal of Sports Medicine

1 2017

1 2003

1 2001

1 Bem S.

1 Boraczyński M.

1 Boraczyński T.

1 Kubicz A.

1 Mila- Kierzenkowska C.

1 Ostrowski W. S.

1 Paprocki J.

1 Pawłowska M.

1 Sopel M.

1 Strzelczyk B.

1 Sutkowy P.

1 Szalewicz A.

1 Woźniak A.

Search results

Effect of tartaric acid on conformation and stability of human prostatic phosphatase: An infrared spectroscopic and calorimetric study.

The 35 kDa acid metallophosphatase of the frog Rana esculenta liver: studies on its cellular localization and protein phosphatase activity.

Wpływ kąpieli w zimnej wodzie na powysiłkową aktywność a1-antytrypsyny i wybranych enzymów lizosomalnych we krwi zdrowych mężczyzn – doniesienia wstępne