[Back to Issue 2 ToC] [Back to Journal Contents] [Back to Biochemistry (Moscow) Home page]
[View Full Article] [Download Reprint (PDF)]

Investigation of Conformational Changes Induced by Binding of Pancreatic RNase to Anti-RNase IgG Derived Fab Monomer Using Optical Procedures

H. Younus1*, S. Jamal1, B. Ahmad1, and M. Saleemuddin1,2

1Interdisciplinary Biotechnology Unit and 2Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, India; fax: +91-571-272-1776; E-mail: hinayounus@rediffmail.com; alg_btisamua@sancharnet.in

* To whom correspondence should be addressed.

Received June 20, 2005; Revision received September 10, 2005
The conformational changes induced in Fab fragments of polyclonal anti-RNase antibody molecules obtained by digestion with papain as a result of binding of pancreatic RNase have been studied. The RNase-Fab complex (RN-Fab), being soluble, could be subjected to thermodynamic investigations using optical strategies, also because of the absence of tryptophan in RNase. Internalization of the chromophores (tryptophans and tyrosines) of Fab occurs when it binds to RNase, suggesting an increase in the compactness of Fab due to the binding of RNase.
KEY WORDS: antigen-antibody complex, Fab, RNase, conformational changes

DOI: 10.1134/S0006297906020155