Fig. 5. Immunoprecipitation analysis of xrds interactions. Triton X- 100 extracts of Xenopus retina were loaded onto columns containing immobilized xrds36, -35, or -38 IgG fractions. After washing, bound xrds proteins were eluted from each column with free xrds36, -35, or -38 peptide. These eluted fractions were analyzed by western blotting with the three xrds peptide antisera. To control for nonspecific aggregation of outer segment membrane proteins, fractions were also analyzed with antiserum against bovine rhodopsin (rho). Note that in each case, the cognate peptide most efficiently eluted its corresponding xrds protein. However, in each case the three xrds proteins co-eluted, with no elution of rhodopsin.
Image published in: Kedzierski W et al. (1996)
Copyright © 1996. Image reproduced with permission of the Publisher, The Company of Biologists Ltd.
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