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Electrophoretic study of papain fragmentation products of walleye pollock and bovine rhod opsins


, : Electrophoretic study of papain fragmentation products of walleye pollock and bovine rhod opsins. Biokhimiya 44(8): 1472-1477

Fragmentation of wall-eyed pollock and bovine rhodopsins by papain in the photoreceptor membrane was studied by sodium dodecyl sulfate electrophoresis. A scheme of step-wise rhodopsin proteolysis is presented. The MW and localization of the carbohydrate and chromophore components of the fragments formed were determined. The photoreceptor membranes of both rhodopsins apparently contain 3 sites accessible to water environment and are indicative of topographical similarity of the rhodopsins.

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Korchagin V.P.; Shukolyukov S.A.; Dikarev V.P., 1979: Electrophoretic investigation of products of fragmentation of pollock and bovine rhod opsin by papain. Biochemistry (Moscow) 44(8 PART 2): 1161-1166

Korchagin, V.P.; Shukoliukov, S.A.; Dikarev, V.P., 1979: Electrophoretic study of products of wall-eyed pollock and bovine rhodopsins fragmented by papain. Fragmentation of wall-eyed pollock and bovine rhodopsins by papain in the photoreceptor membrane was studied by sodium dodecyl sulfate electrophoresis. A scheme of step-wise rhodopsin proteolysis is presented. The molecular weights and localizatio...

Shukolyukov, S.A.; Korchagin, V.P.; Chizhevich, E.P.; Tyurin, V.A., 1977: Poly acrylamide gel electrophoresis of fish walleye pollock and bovine opsins in the presence of sodium dodecyl sulfate. Fish [Theragra chalcogramma] and bovine opsins were found electrophoretically in monomeric forms with some dimers in 1% sodium dodecyl sulfate.sbd.0.05 M sodium phosphate buffer (system I). Opsins have a high tendency to form trimers and higher ol...

Korchagin V.P.; Shukolyukov S.A., 1980: Carbohydrate composition of walleye pollock rhod opsin. Using GLC and column chromatography, the carbohydrate composition of the visual protein rhodopsin from wall-eyed pollock purified by SDS[sodium dodecyl sulfate]-electrophoresis was studied. Similar to bovine rhodopsin, the protein from wall-eyed p...

Shukolyukov, S.A.; Tyurin, V.A.; Korchagin, V.P., 1978: High lability of rhod opsin of the walleye pollock. Stability of rhodopsin of the walleye pollack Theragra chalcogramma to a number of agents and actions (widely used when investigating characteristics of rhodopsins of different animals) was studied. Rhodopsin was partly bleached when the rod outer...

Shukolyukov S.A.; Kalishevich O.O.; Tyurin V.A.; Dikarev V.P.; Korchagin V.P.; Kotelevtsev S.V.; Kagan V.E.; Mitsner B.I.; Sololova N.A., 1980: Chromatography delipidation and formation of recombinants of rhod opsin of the walleye pollock theragra chalcogramma. Biochemistry (Moscow) 45(3 PART 1): 297-304

Shukolyukov S.A.; Kalishevich O.O.; Tyurin V.A.; Dikarev V.P.; Korchagin V.P.; Kotelevtsev S.V.; Kagan V.E.; Mitsner B.I.; Sokolova N.A., 1980: Chromatography de lipidation and formation of rhod opsin phospho lipid recombinants of walleye pollock. Dodecyltrimethylammonium bromide (100 mM) used to solubilize walleyed pollock [Theragra chalcogramma] rhodopsin caused a rapid spontaneous bleaching of the original preparation. Chromatography of the rhodopsin solubilized by 100 mM of N',N&ap...

Shukolyukov, S.A.; Korchagin, V.P.; Fedosov-Yu, V.; Chizhevich, E.P.; Tyurin, V.A., 1976: Rhod opsin extraction amino acid composition and molecular weight in the walleye pollock. Rhodopsin (.lambda.max 500 nm) was extracted from a marine fish Theragra chalcogramma. It was extremely unstable in digitonin, cetyltrimethylammonium bromide (CTAB) and Triton X-100 and quickly bleached at room temperature. The molecular weight of...

Korchagin V.P., 1980: Factors causing oligomerization of walleye pollock rhod opsin before and after solubilization by sodium dodecyl sulfate. Biochemistry (Moscow) 45(6 PART 2): 835-838

Korchagin V.P.; Dikarev V.P.; Shukolyukov S.A., 1978: Fragmentation of rhod opsin by papain. Proteolysis of the rod outer segments (ROS) of the walleyed pollock [Theragra chalcogramma] and bovine results in tight binding of the enzyme by the membranes, resulting in a loss of the enzyme ability to be inhibited by p-chloromercuribenzoate (p...