The interaction of 1-anilino-8-naphthalene sulphonate with erythrocyte membranes
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چکیده
منابع مشابه
Radiation damage to lymphocyte membrane. Changes of binding and fluorescent parameters of 1-anilino-8-naphthalene sulphonate.
The changes of binding and fluorescent parameters of 1-anilino-8-naphthalene sulphonate (ANS) bound to lymphocyte membrane after irradiation in vitro were investigated. No significant dose dependence was found for either fluorescence or its polarization within the dose range of 0.1 to 0.7 Gy from a gamma-neutron field 252Cf source. Marked changes were however found for parameters of ANS binding...
متن کاملStructural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA.
The extrinsic fluorescence dye 8-anilino-1-naphthalene sulfonate (ANS) is widely used for probing conformational changes in proteins, yet no detailed structure of ANS bound to any protein has been reported so far. ANS has been successfully used to monitor the induced-fit mechanism of MurA [UDPGlcNAc enolpyruvyltransferase (EC )], an essential enzyme for bacterial cell wall biosynthesis. We have...
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The interaction of muscle phosphofructokinase with human erythrocyte ghost membranes was investigated. Scatchard analysis of the binding reveals only a single class of binding sites numbering approximately 4 x 10” sites/ghost with an association constant of 2 X lo7 M-‘. Maximum binding is observed below pH 6.8 and is complete within 30 min at 4”, 24”, and 37°C; binding is inhibited by high ioni...
متن کاملThe interaction of phosphofructokinase with erythrocyte membranes.
The interaction of muscle phosphofructokinase with human erythrocyte ghost membranes was investigated. Scatchard analysis of the binding reveals only a single class of binding sites numbering approximately 4 x 10” sites/ghost with an association constant of 2 X lo7 M-‘. Maximum binding is observed below pH 6.8 and is complete within 30 min at 4”, 24”, and 37°C; binding is inhibited by high ioni...
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...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1969
ISSN: 0014-5793
DOI: 10.1016/0014-5793(69)80121-3