Heat-shock response in camel (Camelus dromedarius) blood cells and adaptation to hyperthermia.

1. We demonstrate the difference between the reactions of camel (Camelus dromedarius) lymphocytes and erythrocytes to heat-shock treatment. 2.

Heat shock proteins and thermoresistance in lizards.

The synthesis of heat shock proteins (hsps) at normal physiological and elevated temperatures has been correlated with the natural adaptation of an organism to heat in nine lizard species studied. These species differ drastically by their adaptation to elevated temperature and represent a spectrum of forms isolated from various geographical regions of the Union of Soviet Socialist Republics. The synthesis of hsps belonging to the hsp70 family and their correspondent mRNAs have been compared at different temperature regimes.

[Molecular mechanisms of adaptation to hyperthermia in higher organisms. III. Induction of heat-shock proteins in two Leishmania species].

The heat-shock proteins (hsp) induction in two species of Leishmania have been investigated. The species studied are parasites of two species of lizards (Lymnodactylus caspins and Agama caucasica) differing by temperature of correspondent ecological niche. Our results show that Leishmania species restricted to high-temperature host (Agama) is capable to synthesize its proteins at extreme temperatures (38, 40 degrees C) with greater intensity.

[Properties of the cell-free protein synthesizing system from the fibroin region of the Bombyx mori silkgland].

Microsomes isolated from the fibroin region of the Bombyx mori silkgland synthesize in the cell-free system a glycin rich polypeptide or polypeptides presumably representing fibroin precursors. Besides microsomes the system requires ATP and ATP-generating system, GTP, soluble protein fraction and tRNA, glycine incorporation is inhibited by puromycin and cycloheximide. It is shown that the synthesis of a polypeptide with high Gly/Lys ratio requires soluble protein fraction isolated from the silk gland at the end of the instar V.