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Proteolytic susceptibility and methionine modification of monodeamidated ribonuclease A

Das , MK and Vithayathil, PJ (1978) Proteolytic susceptibility and methionine modification of monodeamidated ribonuclease A. In: International Journal of Peptide & Protein Research, 12 (5). pp. 242-248.

Full text not available from this repository.
Official URL: http://www.ncbi.nlm.nih.gov/pubmed/370043

Abstract

The susceptibility of a monodeamidated RNAaseA (RNAaseAa1) towards carboxypeptidaseA , alpha-chymotrypsin and pepsin has been studied. Similar to RNAaseA, the C-terminal of RNAaseAa1 is not available for carboxypeptidaseA hydrolysis. The thermal stability of RNAaseAa1 as probed through chymotryptic digestion is found to be less than that of RNAaseA. Preliminary chromatographic analysis of the digested material, however, suggests that the nature of thermal transition might be the same in the two proteins. Pepsin inactivates RNAaseAa1 more slowly than does RNAaseA. Accordingly, less peptide bonds, almost half that of RNAaseA, are cleaved by pepsin in RNAaseAa1. The accumulation of RNAase-P type intermediates is not evident during peptic digestion of RNAaseAa1. Reaction with O-benzoquinone at low pH shows that methionines of the deamidated protein seem to have higher reactivities. These observations indicate a different structure for RNAaseAa1 at elevated temperature and low pH.

Item Type: Journal Article
Additional Information: Copy right of this article belongs to National Center for Biotechnology Information.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 29 Sep 2010 11:23
Last Modified: 29 Sep 2010 11:23
URI: http://eprints.iisc.ernet.in/id/eprint/32521

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