Calcium binding by human erythrocyte membranes
نویسندگان
چکیده
منابع مشابه
Calcium binding capacity of erythrocyte membrane in human hypertension.
The cell membrane calcium binding capacity of genetically hypertensive rats is reduced when measured in the presence of the submicromolar calcium concentrations proper of intracellular environment. The present work, performed as an ancillary study to an epidemiological survey on an entire population, aimed to investigate the existence of a similar abnormality in human hypertension. Calcium bind...
متن کاملCalcium Binding to Intestinal Membranes
Flame photometry reveals that glutaraldehyde and buffer solutions in routine use for electron microscopy contain varying amounts of calcium. The presence of electron-opaque deposits adjacent to membranes in a variety of tissues can be correlated with the presence of calcium in the fixative. In insect intestine (midgut), deposits occur adjacent to apical and lateral plasma membranes. The deposit...
متن کاملSolubilization of human erythrocyte membranes by ASB detergents.
Understanding the membrane solubilization process and finding effective solubilizing agents are crucial challenges in biochemical research. Here we report results on the interaction of the novel linear alkylamido propyl dimethyl amino propanosulfonate detergents, ASB-14 and ASB-16, with human erythrocyte membranes. An estimation of the critical micelle concentration of these zwitterionic deterg...
متن کاملVitamin E recycling in human erythrocyte membranes.
Vitamin E, the major lipid chain-breaking antioxidant in erythrocyte membranes, is present in low concentration, suggesting that mechanisms should exist to protect against its loss. Enzymatic pathways for the recycling of vitamin E from its tocopheroxyl radical have been observed previously in inner membranes of mitochondria and microsomes. These pathways use electron transport enzymes and thei...
متن کاملInteraction of bilirubin with human erythrocyte membranes.
The kinetics of [3H]bilirubin binding to human erythrocyte ghost membranes was investigated. The binding occurred rapidly and was saturable with respect to [3H]bilirubin and membrane concentration. The apparent dissociation constant (Kd) and maximum binding (Bmax.) for bilirubin of the membranes were 2.3 microM and 0.93 nmol/mg of protein respectively. Low-affinity binding, non-saturable at 400...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1971
ISSN: 0306-3283
DOI: 10.1042/bj1240563