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Selective stabilization of a labile mutant form of bovine pancreatic ribonuclease A by antibodies

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Abstract

The region between the amino acids 31-46 was previously identified as being first exposed during thermal unfolding of bovine pancreatic ribonuclease A (RNase). The exchange of one amino acid (Leu35toSer) in this unfolded region of RNase is shown to have a dramatic destabilizing effect (ΔTm=9 °C). Antibodies raised against a peptide corresponding to the sequence of the labile region, S32-V43, of RNase were effective in stabilizing L35S-RNase against thermal inactivation (65 °C for 2 h) and surpassed the stabilization effect of antiRNase antibodies. An 11% contribution to the stabilizing effect of antiRNase antibodies resulted from antibodies recognizing the unfolding region of the enzyme.

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Younus, H., Köditz, J., Saleemuddin, M. et al. Selective stabilization of a labile mutant form of bovine pancreatic ribonuclease A by antibodies. Biotechnology Letters 24, 1821–1826 (2002). https://doi.org/10.1023/A:1020642112487

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  • DOI: https://doi.org/10.1023/A:1020642112487

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