New approach to the study of hormone-protein interaction using the microcalorimetric method. |
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Authors: | J Kniewald Z Kniewald P Mildner |
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Institution: | 1. Institute for Physical Chemistry, University of Zagreb, 41000 Zagreb, Yugoslavia;2. Laboratory for Experimental Medicine, University of Zagreb, 41000 Zagreb, Yugoslavia;3. Laboratory for Biochemistry, Faculty of Technology, University of Zagreb, 41000 Zagreb, Yugoslavia |
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Abstract: | Binding enthalpies of various hormones to bovine serum albumin (BSA) and human serum albumin (HSA) in 50 mM phosphate buffer, pH 7.4, at 37 degrees C have been determined by direct microcalorimetry. The observed enthalpies of binding of progesterone, testosterone, dihydrotestosterone, corticosterone and estriol to BSA were found to be -13.24 plus or minus 0.11 -10.31 plus or minus 0.02, -2.37 plus or minus 0.46, -17.64 plus or minus 0.32 and -17.14 plus or minus 0.36 kcal/mol of hormone, respectively. under the same experimental conditions the enthalpies of binding of progesterone, testosterone, dihydrotestosterone, corticosterone and estriol to HSA were found to be -23.94 plus or minus 0.32, -18.88 plus or minus 0.49, -11.14 plus or minus 0.02, -9.88 plus or minus 0.14 and -20.85 plus or minus 0.39 kcal/mol of hormone, respectively. |
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Keywords: | Corticosterone 11β 21-Dihydroxy-4-pregnene-3 20-dione Dihydrotestosterone 17β -Hydroxy-5α -androstan-3-one Estriol 1 3 5 (10) -Estratriene-3 16 α 17β -triol Progesterone 4-Pregnene-3 20-dione Testosterone 17β -Hydroxy-4-androsten-3-one BSA bovine serum albumin HSA human serum albumin |
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