The reactivity of p-nitrophenyl acetate with serum albumins.
1. Serum albumins from nine of 10 vertebrate species were found to react rapidly with p-nitrophenylacetate. 2. The high reactivities were shown to be partially attributable to strong, rapidly reversible binding of p-nitrophenylacetate by each serum albumin. 3. As previously observed in the case of human serum albumin (Koh and Means, Arch. Biochem. Biophys. 192, 73-79, 1979), this binding takes place in the primary binding site for several physiologically (i.e. tryptophan, small fatty acid anions) and pharmacologically (i.e. diazepam) important compounds. 4. Horse serum albumin differed from all other serum albumins included in this study in that it did not react rapidly with p-nitrophenylacetate, presumably, due to significant differences in its corresponding binding site.
Awad-Elkarim
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Department of Biochemistry, Ohio State University, Columbus 43210.
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D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D009596:Nitrophenols / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013045:Species Specificity; D014714:Vertebrates
D009596:Nitrophenols; D012709:Serum Albumin; C008642:4-nitrophenyl acetate