Solubilization of human erythrocyte membrane glycoproteins by triton X-100
نویسندگان
چکیده
منابع مشابه
Differential solubilization of inner plasma membrane leaflet components by Lubrol WX and Triton X-100.
A commonly-used method for analysing raft membrane domains is based on their resistance to extraction by non-ionic detergents at 4 degrees C. However, the selectivity of different detergents in defining raft membrane domains has been questioned. We have compared the lipid composition of detergent-resistant membranes (DRMs) obtained after Triton X-100 or Lubrol WX extraction in MDCK cells in ord...
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In this study the application of ZnO nanoparticles to UV photocatalytic degradation of nonionic surfactantTriton X-100 in aqueous media was investigated. The affecting factors on the photodegradation such as TritonX-100 initial concentration, nanocatalyst weight, pH, temperature and other parameters were studied anddescribed in details. The degradation rate was found to be strongly influenced b...
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To identify integral and peripheral membrane proteins, highly purified coated vesicles from bovine brain were exposed to solutions of various pH, ionic strength, and concentrations of the nonionic detergent Triton X-100. At pH 10.0 or above most major proteins were liberated, but four minor polypeptides sedimented with the vesicles. From quantitative analysis of phospholipids in the pellet and ...
متن کاملFurther studies on the interaction between human platelet membrane glycoproteins IIb and IIIa in triton X-100.
Analysis of human platelet membrane proteins by crossed immunoelectrophoresis (CIE) in the presence of Triton X-100 (TX-100) has previously shown that glycoproteins (GP) IIb and IIIa are located in a single immunoprecipitate, band 16.2 To investigate whether IIb and IIIa are associated in a complex, we have analyzed TX-100-solubilized 125I-labeled membrane proteins by density gradient ultracent...
متن کاملFurther Studies on the Interaction Between Human Platelet Membrane Glycoproteins lib and lila in Triton X - 100
labeled membrane proteins by density gradient ultracentrifugation using 1 O%-40% sucrose gradients containing the nonionic detergent. Studies were performed using soluble proteins derived from membranes isolated in the presence or absence of EDTA. Analysis of gradient fractions by SDS-polyacrylamide gel electrophoresis showed that in the absence of divalent cation chelation. GP lIb and lIla pen...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1979
ISSN: 0264-6021
DOI: 10.1042/bj1790299