Physico-chemical properties of acetylcholine receptor proteins from Narke japonica.
The molecular weights of acetylcholine receptor proteins from Narke japonica were determined using a combination of high-speed gel filtration and the low angle laser light scattering technique. The values obtained were 460,000 and 240,000 for the dimer and monomer, respectively. By use of a weakly charged silica gel column for high-speed gel filtration calibrated by considering electrostatic interactions between proteins and gel surfaces, the Stokes radii of the proteins were estimated as 7.3 nm and 6.2 nm. Chromatography in 6 M guanidine hydrochloride (GmHCl) showed that the proteins were hardly dissociated to subunits, and CD measurements confirmed that the proteins are resistant to GmHCl denaturation. These results suggest that strong hydrophobic interactions exist among the receptor subunits and probably within the subunits themselves.
D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002850:Chromatography, Gel; D002942:Circular Dichroism; D004557:Electric Organ / Q000032:analysis*; D005399:Fishes; D006146:Guanidines / Q000032:analysis; D008970:Molecular Weight; D011950:Receptors, Cholinergic / Q000032:analysis*; D014461:Ultracentrifugation
D006146:Guanidines; D011950:Receptors, Cholinergic