Effect of tartaric acid on conformation and stability of human prostatic phosphatase: an infrared spectroscopic and calorimetric study.
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 degrees 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.
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Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland.
Ostrowski
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D000135:Acid Phosphatase; D002152:Calorimetry, Differential Scanning; D006801:Humans; D011487:Protein Conformation / Q000187:drug effects; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry* / Q000378:metabolism*; D013055:Spectrophotometry, Infrared; D013644:Tartrates / Q000494:pharmacology*; D013696:Temperature
D013644:Tartrates; D000135:Acid Phosphatase; C428439:prostatic acid phosphatase; D017027:Protein Tyrosine Phosphatases; C029768:tartaric acid