Further Studies on the Interaction Between Human Platelet Membrane Glycoproteins lib and lila in Triton X - 100
نویسندگان
چکیده
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 penetrated well into the gradient (fractions 1 5-i 7). Analysis of
منابع مشابه
Further 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...
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We have previously demonstrated the isolation of platelet membrane glycoprotein lIb-Illa by affinity chromatography with a specific monoclonal antibody.1 We have now separated the polypeptide subunits lIb and lIla of the isolated glycoprotein by preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis and have compared their structural features. Both llb and lIla contain -.1 5% car...
متن کاملFurther Studies on the Interaction Between Human Platelet Membrane Glycoproteins
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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