Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2015 Dec 15;44(2):801–810. doi: 10.1093/nar/gkv1469

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

PMC Copyright notice

Figure 4. — Formation of methyl O-glycoside site in DNA. (A) The hydrolysis product AP site (left path) undergoes β/δ-elimination upon treatment with sodium hydroxide (NaOH). Conversely, the methanolysis product (right path) is resistant to cleavage by NaOH. (B) HPLC traces for methanolysis reactions with Gs MutY (solid) and without enzyme (dashed) indicate baseline separation of all substrates and products and verify that all products are generated by an enzyme-catalyzed reaction. (C) MALDI-MS confirms the presence of a dROMe-oligomer (predicted 3213.1 Da, measured 3216.9 Da, +3.8 offset).