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JBC, Vol. 254, Issue 22, 11242-11246, Nov, 1979
N. V. Costrini, M. Kogan, K. Kukreja and R. A. Bradshaw
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.
Physical properties of the detergent-extracted nerve growth factor receptor of sympathetic ganglia
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