Abstract
The histone H1 of Ceratitis capitata has been digested with thrombin and three of the resulting peptides (TC-1, TC-3 and TC-4) have been isolated and compared with those obtained from calf H1. TC-1 contains part of the N- terminal region of the H1 molecule as well as a significant portion of the globular head. CD 1 measurements suggest that most of the residues of the H1 molecule that fold to a ordered secondary structure are present in TC-1. TC-3 and TC-4 come from the C-terminal region of the H1 molecule, the former containing some residues from the globular head. Neither TC-3 nor TC-4 are able to fold on increasing ionic strength.
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.
