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2001 | 48 | 3 | 755-762
Article title

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

Content
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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.
Publisher

Year
Volume
48
Issue
3
Pages
755-762
Physical description
Dates
published
2001
received
2001-04-23
revised
2001-05-16
accepted
2001-08-29
Contributors
author
  • Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland
  • Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland
References
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv48i3p755kz
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