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

• Autorzy: Bem S. , Ostrowski W.S.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

differential scanning calorimetry; Fourier transform infrared spectroscopy; conformation; acid phosphatase; prostatic phosphatase; man; tartaric acid; stability; tartrate; prostate; secondary structure

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2001
• Tom: 48
• Numer: 3
• Opis fizyczny: p.755-762,fig.

Twórcy

autor

Bem S.

• Jagiellonian University, M.Kopernika 7, 31-034 Krakow, Poland

autor

Ostrowski W.S.

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