Abstract
Characterization of detergent-solubilized membrane proteins. Hydrodynamic and sedimentation equilibrium properties of the insulin receptor of the cultured human lymphoblastoid cell.
Highlights
From the Departments of Medicine and Biochemistry, University of South Florida and Veterans Administration Medical Centers, Tampa, Florida 33612
IM-9 was solubilizedwith the nonionic detergent Triton ing a high degree of molecular asymmetry, X-100.Scatchard analysis of insulin binding revealed a confirmation of the high level of hydration of the bound homogeneous class of noncooperative binding sites detergent indicates that the asymmetry component of with K, = 2 X lo8M-’, corresponding to thehigh affinity the frictional ratio ( ( f / f o ) =~ 1.2) for these complexes component of cellular insulin binding
The characterization of small quantities of biological macromolecules having a specific measurable biochemical activity or derivative thereof has been somewhat limited by the empirical bases of available techniques, including sedimentation interpreting empirically derived hydrodynamic data, through sucrose gradients [1,2,3], gel fitration chromatography the sedimentation equilibrium behavior of the deter- (4, 5 ), and a sodium dodecyl sulfate-polyacrylamide gel elecgent-solubilized receptor covalently cross-linked to trophoresis ( 6 4, by anomalous behavior [6, 8, 9], and by
Summary
From the Departments of Medicine and Biochemistry, University of South Florida and Veterans Administration Medical Centers, Tampa, Florida 33612. The high affinity insulin receptor from the plasma receptor and many other detergent-membrane protein membrane of the cultured human lymphoblastoid cell complexes has been previously interpreted as reflect-. The characterization of small quantities of biological macromolecules having a specific measurable biochemical activity or derivative thereof has been somewhat limited by the empirical bases of available techniques, including sedimentation interpreting empirically derived hydrodynamic data, through sucrose gradients [1,2,3], gel fitration chromatography the sedimentation equilibrium behavior of the deter- (4, 5 ) , and a sodium dodecyl sulfate-polyacrylamide gel elecgent-solubilized receptor covalently cross-linked to trophoresis
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