Physical properties of the detergent-extracted nerve growth factor receptor of sympathetic ganglia.
The nerve growth factor (NGF) receptor from microsomes of adult rabbit superior cervical ganglia has been solubilized with Triton X-100 and sodium deoxycholate. The physical properties of the detergent-extracted NGF receptor were assessed by Sepharose 6B chromatography and sucrose density gradient ultracentrifugation studies in H2O and D2O. The predominant form of the NGF receptor has a Stokes radius of 71 A, a partial specific volume of 0.74 ml/g, a sedimentation coefficient of 4.3 S, and a frictional ratio of 1.8. From these parameters, it can be calculated that the NGF receptor in Triton X-100 is a minimally hydrophobic, highly asymmetric, intrinsic membrane protein with a molecular weight of approximately 135,000. A form of the receptor with a sedimentation coefficient of 10.4 S was occasionally seen which appears to represent an aggregated form of the 4.3 S moiety.
D000818:Animals; D002499:Centrifugation, Density Gradient; D005728:Ganglia, Sympathetic / Q000378:metabolism*; D008565:Membrane Proteins / Q000302:isolation & purification; D008970:Molecular Weight; D009414:Nerve Growth Factors / Q000378:metabolism*; D011487:Protein Conformation; D011817:Rabbits; D011955:Receptors, Drug / Q000302:isolation & purification / Q000378:metabolism
D008565:Membrane Proteins; D009414:Nerve Growth Factors; D011955:Receptors, Drug