LINKER HISTONE-DNA COMPLEXES - ENHANCED STABILITY IN THE PRESENCE OF ALUMINUM LACTATE AND IMPLICATIONS FOR ALZHEIMERS-DISEASE
LINKER HISTONE-DNA COMPLEXES - ENHANCED STABILITY IN THE PRESENCE OF ALUMINUM LACTATE AND IMPLICATIONS FOR ALZHEIMERS-DISEASE
复制标题
DOI：
10.1016/0014-5793(89)80929-9
复制
发表时间：
1989-08-14
期刊：
影响因子：
3.5
通讯作者：
MCLACHLAN, DR
中科院分区：
文献类型：
--
作者：
LUKIW, WJ;KRUCK, TPA;MCLACHLAN, DR
The binding of human brain linker histone proteins to a radiolabelled human Alu repetitive element was examined by mobility shift assay.. Analysis of the complexes formed from protein extracts of whole neocortical nuclei, under physiological conditions in vitro revealed that linker histone H1° has the highest affinity for the Alu DNA sequence. The linker histone‐DNA complexes assembled in the presence of aluminum lactate were more resistant to sodium chloride‐induced dissociation than those formed in the presence of sodium lactate. The enhanced stability of deoxyribonucleoprotein (DNP) complexes in the presence of the aluminum cation may be of significance in neurodegenerative conditions such as Alzheimer's disease where aluminum preferentially associates with DNA containing structures of the nucleus.
