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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

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

Volume 13, Issue 7, 2006

Page: [673 - 677] Pages: 5

DOI: 10.2174/092986606777790629

Price: $65


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.

Keywords: ribonuclease A, antibodies, aggregation inhibition

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