[New 26 kDa protein specific for photoreceptor cells, capable of binding with immobilized delipidized rhodopsin]. / Novyy spetsifichnyi dlia fotoretseptornykh kletok belok s molekuliarnoi massoi 26 kDa, sposobnyi sviazyvat'sia s immobilizvannym delipidizirovannym rodopsinom.

A protein p26 with molecular weight 26 kDa capable of binding to delipidated rhodopsin immobilized on Concanavalin A-Sepharose was found in photoreceptor cells of bovine retina. Mono specific antibodies against this protein were used to demonstrate this protein to be located in a layer of photoreceptor cells, both in their inner and outer segments. On the basis of its antigenic properties p26 is different from any other known photoreceptor cells-specific proteins.

[A study of the interaction of immobilized delipidized rhodopsin with G-proteins]. / Izuchenie vzaimodeistviia immobilizovannogo delipidizirovannogo rodopsina s G-belkami.

It was shown that delipidated rhodopsin immobilized on concanavalin A-Sepharose (Rimm) binds with high selectivity transducin from total extracts of rod outer segment protein as well as the regulatory GTP-binding Gi- and Go-like proteins from solubilized membranes of bovine brain. The Rimm-bound proteins are eluted in the presence of the nonionic detergent, octyl glucoside, and GTP. This suggests that Rimm can be used as an affinity adsorbent for the isolation and purification of G-proteins.