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. Author manuscript; available in PMC: 2006 Feb 10.
Published in final edited form as: Methods Enzymol. 2002;343:578–600. doi: 10.1016/s0076-6879(02)43159-x

Fig. 3.

Fig. 3

Molecular rules of opsin activation: phosphorylation of opsin in the presence of all-trans-retinal analogs of different lengths and their derivatives with blocked aldehyde groups. (A) Phosphorylation of opsin is carried out in the presence of all-trans-retinal, all-trans-C17 aldehyde, all-trans-C15 aldehyde, trans-C12 aldehyde, or their oximes generated with NH2OH, NH2OCH3, or NH2OCH2CH3 (8 M excess over 30 μM opsin). The solid horizontal line represents opsin activity. (B) Activity expressed as percentage of maximum phosphorylation for each of the aldehydes (marked as a continuous line). The phosphorylation reaction is carried out in 30 mM BTP, pH 6.5, containing 3 mM MgCl2. Data are reproduced with permission from the American Society for Biochemistry and Molecular Biology, Inc. [J. Buczyłko, J. C. Saari, R. K. Crouch, and K. Palczewski, J. Biol. Chem. 271, 20621 (1996)]. (C) Structures of all-trans-retinal, all-trans-C17 aldehyde, all-trans-C15 aldehyde, trans-C12 aldehyde.