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

• Authors: Sławomir Bem , Włodzimierz S Ostrowski
• Languages of publication: EN

Abstracts

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.

Keywords

EN

secondary structure; prostate; acid phosphatase; tartrate

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2001
• Volume: 48
• Issue: 3
• Pages: 755-762

Dates

published

2001

received

2001-04-23

revised

2001-05-16

accepted

2001-08-29

Contributors

author

Sławomir Bem

• Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland

author

Włodzimierz S Ostrowski

• Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland

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