منابع مشابه
Fractionation of the protein components of human erythrocyte membranes.
The proteins of the human erythrocyte membrane can be fractionated into several groups. Approximately one-half of the proteins in the membrane can be removed by sequential extraction of the erythrocyte ghost, first with a solution containing chelating agents, and then with concentrated NaCl solutions. A small amount of the membrane proteins (less than 10% of the total proteins) remains in the o...
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 کاملAnionic Sites of Human Erythrocyte Membranes
The effects of pH, trypsin, and phospholipase C on the topographic distribution of acidic anionic residues on human erythrocytes was investigated using colloidal iron hydroxide labeling of mounted, fixed ghost membranes. After glutaraldehyde fixation at pH 6.5-7.5, the positively charged colloidal particles were bound to the membranes in small randomly distributed clusters. The clusters of anio...
متن کاملAdriamycin induces protein oxidation in erythrocyte membranes.
Adriamycin is an anthracycline antineoplastic agent whose clinical effectiveness is limited by severe side effects, including cardiotoxicity. A current hypothesis for adriamycin cardiotoxicity involves free radical oxidative stress. To investigate this hypothesis in a model system, we applied the technique of immunochemical detection of protein carbonyls, known to be increased in oxidized prote...
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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1968
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)93538-6