Effects of drug-binding on the thermal denaturation of human serum albumin
Asymmetric thermograms of defatted albumin, alone and in the presence of two model drugs, have been obtained in phosphate buffers at three pH values. The albumin is less thermally stable in the N form, but is protected by both drugs. The nonsteroidal antiinflammatory benoxaprofen offers more protect...
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| Published in | Journal of pharmaceutical and biomedical analysis Vol. 12; no. 12; p. 1501 |
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| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
01.12.1994
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| Subjects | |
| Online Access | Get more information |
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| Abstract | Asymmetric thermograms of defatted albumin, alone and in the presence of two model drugs, have been obtained in phosphate buffers at three pH values. The albumin is less thermally stable in the N form, but is protected by both drugs. The nonsteroidal antiinflammatory benoxaprofen offers more protection than warfarin against thermal denaturation. |
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| AbstractList | Asymmetric thermograms of defatted albumin, alone and in the presence of two model drugs, have been obtained in phosphate buffers at three pH values. The albumin is less thermally stable in the N form, but is protected by both drugs. The nonsteroidal antiinflammatory benoxaprofen offers more protection than warfarin against thermal denaturation. |
| Author | Esser, A F Sen, A C Perrin, J H Lohner, K Prankerd, R |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/7696374$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | Anti-Inflammatory Agents, Non-Steroidal - pharmacology Binding Sites Calorimetry, Differential Scanning Humans Propionates - pharmacology Protein Denaturation Serum Albumin - chemistry Warfarin - pharmacology |
| Title | Effects of drug-binding on the thermal denaturation of human serum albumin |
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