Abstract
Thymus chromatin was extensively modified with ethyl acetimidate, substituting up to 90% of the lysyl residues of the histones while retaining the positive charge of the basic amino acid. Physiochemical and immunochemical characterization of this derivative chromatin indicates a high degree of retention of the native structure of the nucleoprotein even after extensive modification. The alterations which are detected are most simply interpreted as resulting from a weakening of the interactions of histone H1 with DNA in the modified chromatin. The near-native character of amidinated chromatin contrasts with the more extensive structural alterations observed in acetylated chromatin. Our data demonstrate the suitability of this reagent for mapping available lysyl residues in this and other nucleoproteins and suggest that the related bisimido esters may be reagents of choice for cross-linking of chromatin histones.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
