Inhibition of pancreatic ribonuclease A aggregation by antibodies raised against the native enzyme and its N-terminal dodecapeptide.
Pancreatic ribonuclease A (RNase A) has been shown to aggregate moderately and gradually at 65 degrees 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 degrees 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.
Younus
Hina
H
Interdisciplinary Biotechnology Unit, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, India.
Ulbrich-Hofmann
Renate
R
Saleemuddin
Mohammad
M
D000818:Animals; D000906:Antibodies / Q000378:metabolism*; D002417:Cattle; D009842:Oligopeptides / Q000276:immunology*; D011817:Rabbits; D012259:Ribonuclease, Pancreatic / Q000037:antagonists & inhibitors* / Q000276:immunology*
D000906:Antibodies; D009842:Oligopeptides; D012259:Ribonuclease, Pancreatic