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- W2045499867 abstract "The conformational equilibrium constant, Kconf, of staphylococcal nuclease, describing the equilibrium between the native conformation and non-native or disordered conformations, has been estimated using an immunologic method and an interpretive model. Using goat antisera prepared toward a conformationally disordered nuclease fragment (99–149), antibodies specific for the disordered form of the helix-rich sequence 99 to 126, anti-(99–126)R, were isolated by sequential immunoabsorption. Anti-(99–126)R forms soluble 7 S complexes with fragment (99–149), but this interaction may be inhibited by a large excess of nuclease. By using fragment (99–149) preferentially carbamylated at the α-amino terminus with KN14CO and rabbit anti-goat immunoglobulin to distinguish between antibody-bound and free fragment (99–149), an assay for the quantitation of the degree of inhibition of anti-(99–126)R. (99–149) complex formation by nuclease was developed. Using a formal analysis based on the hypothesis that nuclease is in a conformational equilibrium between a folded and unfolded form and that anti-(99–126)R binds effectively only to the unfolded form, the Kconf of nuclease was estimated to be 2900. In the presence of the ligands Ca(II), or Ca(II) and thymidine-3′,5′-diphosphate, Kconf values of 6500 and 30,000 to 50,000 were estimated, respectively. The Kconf of nuclease at 4 °C and 39 °C was 3900 and 400, respectively." @default.
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- W2045499867 date "1975-03-01" @default.
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- W2045499867 title "An immunological approach to the conformational equilibrium of staphylococcal nuclease" @default.
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- W2045499867 doi "https://doi.org/10.1016/0022-2836(75)90305-8" @default.
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