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

S Bem | Zendy; W Ostrowski | Zendy

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

Author(s) -

S Bem,

W Ostrowski

Publication year - 2001

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2001_3910

Subject(s) - tartaric acid , differential scanning calorimetry , fourier transform infrared spectroscopy , chemistry , infrared , thermal stability , infrared spectroscopy , acid phosphatase , thermal analysis , analytical chemistry (journal) , crystallography , thermal , chromatography , biochemistry , organic chemistry , chemical engineering , enzyme , thermodynamics , optics , physics , engineering , citric acid

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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