Accession Number : ADA294362
Title : Third and Final Technical Report for F49620-92-0232-DEF (San Francisco State University).
Descriptive Note : Final technical rept. 1 Apr 94-31 Mar 95,
Corporate Author : SAN FRANCISCO STATE UNIV TIBURON CA ROMBERG TIBURON CENTERS
Personal Author(s) : Kun, Ernest
PDF Url : ADA294362
Report Date : 29 APR 1995
Pagination or Media Count : 137
Abstract : Cellular proteins extracted from normal and cancer cells bind poly(ADP-ribose) polymerase on nitro-cellulose membrane transblots. Histones at 1 rng/ml concentration completely prevent the binding of poly(ADP-ribose) polymerase to cellular proteins, indicating that the binding of histones to poly(ADP-ribose) polymerase sites competitively blocks the association of poly (ADP-ribose) polymerase to proteins other than histones. The direct binding of poly(ADP-ribos polymerase to histones is shown by crosslinking with glutaraldehyde. The C-terminal basic histone Hi tail binds to the basic polypeptide domain of poly(ADP-ribose) polymerase. The basic domain present in the N-terminal part of core histones is the probable common structural feature of all core histones that accounts for their binding to poly(ADP-ribose) polymerase. Two polypeptide domains of poly(ADP-ribose) polymerase were identified, by way of CNBr fragments, to bind histones.
Descriptors : *CELLS, *POLYMERIZATION, *CANCER, CORES, STRUCTURAL PROPERTIES, PEPTIDES, POLYMERS, ENZYMES, PROTEINS, PROBABILITY, DEOXYRIBONUCLEIC ACIDS, IN VITRO ANALYSIS, IN VIVO ANALYSIS, AMINO ACIDS, HISTONES, RIBOSE.
Subject Categories : Polymer Chemistry
Medicine and Medical Research
Distribution Statement : APPROVED FOR PUBLIC RELEASE