Inhibition of Pancreatic Ribonuclease A Aggregation by Antibodies Raised Against the Native Enzyme and Its N-Terminal Dodecapeptide

Title: Inhibition of Pancreatic Ribonuclease A Aggregation by Antibodies Raised Against the Native Enzyme and Its N-Terminal Dodecapeptide

Volume: 13 Issue: 7

Author(s): Hina Younus, Renate Ulbrich-Hofmann and Mohammad Saleemuddin

Affiliation:

Keywords: ribonuclease A, antibodies, aggregation inhibition

Abstract: Pancreatic ribonuclease A (RNase A) has been shown to aggregate moderately and gradually at 65°C. Antibodies raised against the dodecapeptide KETAAAKFERQG corresponding to the N-terminal 1-12 amino acid residues of RNase A (Npep) as well as native RNase A were effective in lowering RNase A aggregation at 65°C. The antiRNase A antibodies were, however, more protective. The binding of antiNpep antibodies to the N-terminal region of RNase A may interfere with initiation of oligomerization of the enzyme and consequently its aggregation. The antiRNase A antibodies were presumably more effective in protecting RNase A against aggregation by binding to multiple epitopes of the enzyme including the N-terminal region and hence restricting the interaction of the monomers.

Cite this article as:

Younus Hina, Ulbrich-Hofmann Renate and Saleemuddin Mohammad, Inhibition of Pancreatic Ribonuclease A Aggregation by Antibodies Raised Against the Native Enzyme and Its N-Terminal Dodecapeptide, Protein & Peptide Letters 2006; 13(7) . https://dx.doi.org/10.2174/092986606777790629