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S A Suvorov

Publications and source records attributed to S A Suvorov.

6 recordsLinked to original sources
PubMed1984

[The presence of calmodulin in chemosensory structures, its purification and content].

Chemosensory tissues, bovine olfactory epithelium and barbel of dwarf sheat-fish (Ictalurus nebulosus) rich in gustatory buds were shown to contain calmodulin. The fraction of thermostable proteins which activate brain phosphodiesterase of cyclic nucleotides was purified to homogeneity by stepwise ion-exchange chromatography on DEAE-cellulose and gel filtration on Sephacryl S-300. Some properties of calmodulin from chemosensory tissues (e. g., content, molecular weight, electrophoretic mobility, degree of activation of phosphodiesterase) are similar to those of brain calmodulin.

2',3'-Cyclic-Nucleotide Phosphodiesterases↗
PubMedDate not supplied

[Thermal stability of rhodopsins and opsins in warm- and cold-blooded vertebrates].

Thermal stability of rhodopsins and opsins has been studied in endothermic (sheep, cattle, pig, rat) and ectothermic (frog) animals under two different conditions -- in the intact photoreceptor membranes (PM) and after substitution of the lipid surrounding of rhodopsins by molecules of a detergent Triton X-100. Lipid composition of PM in these animals was also studied, as well as the effect of proteases (pronase and papaine) upon thermal stability of rhodopsins in PM and in 1% Triton X-100 solutions. The thermal resistance of rhodopsins in PM was found to vary in the animals used to a great extent. The maximal differences in thermal stability of rhodopsins in ecto- and endothermic animals were due to the properties of photoreceptor protein itself, whereas in ectothermic animals they resulted mainly from differences in the lipid composition of PM. PM of endothermic animals differ from those of ectothermic ones by a lower content of polyenoic fatty acids and by a higher amount of phosphatidyl ethanolamine. The thermal stability of rhodopsins is not due to rhodopsin molecule as a whole, and depends mainly on its part which is directly bound to 11-cis retinal, located in hydrophobic region of PM and inaccessible to protease attack.

Animals↗