[Stress proteins in the cells of Porphyra purpurea (Rhodophyta) thallus].

Heat shock proteins have been revealed for the first time by the methods of Western blotting using alkaline phosphatase and ECL in the cells of Porphyra purpurea from Kattegat area of the Baltic Sea in normal and experimental stress conditions. It was demonstrated with application of monoclonal anti-Hsp70 antibodies that a slight band about 70 kDa is present constitutively at the film; additionally the polypeptide of about 40 kDa ("Hsp40") has been detected. After heat shock at 28 degrees C during 1 hr significant "expenditure" of Hsp70 was observed, as well as the pronounced induction of "Hsp40"; the induction was expressed especially strongly in 24 hr after the stress application.

[Changes of heat shock proteins content in the gill epithelium cells of mussel Mytilus edulis L. depending upon the salinity of medium].

The composition and the level of heat shock (stress) proteins content were studied by the method of immunobloting in the gill epithelium cells of mussels Mytilus edulis L. from the White sea, treated by water of different salinities. Stress proteins of about 70 and 40 kDa were revealed at Western blots.

[Heat shock proteins of 70 kDa family in the cells of free living and amphizoic amoeboid organisms].

The content of constitutive from of 70 kDa family heat shock pritein (Hsp70) was determined by the method of immunoblotting. 9 strains of representatives of the genus Acanthamoeba including 8 amphizoic (facultative parasitic) strains and one free-living (isolated from upper horizons of Arctic soils) were studied. We also examined 15 strains of free-living freshwater amoebae of various geographic origin, age and species.

[Correlations between salinity-persistence of ciliate species and their constitutive heat shock protein of 70 kDa contents].

Our own studies of alterations in the level of constitutive heat shock protein of 70 kDa family (Hsp70) in freshwater (Paramecium jenningsi), meta-freshwater (Tetrahymena pyriformis) and curyhaline (P. nephridiatum) ciliates acclimated to salt-water and fresh-water medium were reviewed. It has been shown that the level of constitutive Hsp70 content correlates with the salinity-resistance of ciliate species: in P.

[Alterations of the level of 70 kDa family heat shock protein in the ciliate Tetrahymena pyriformis in the process of the cells adaptation to the medium salinity changes].

Alterations of Hsp70 level were studied in the cells of freshwater ciliate Tetrahymena pyriformis after medium salinity changes. It is shown that ciliates, acclimated to fresh water (0 per thousand) and to salt water of 2 and 10 per thousand have similar constitutive levels of Hsp70 in their cells. Neither pronounced induction of Hsp70, was not decrease of its level, revealed in ciliates after salinity stresses.

[Expression of stress proteins of family HSP70 in response to cold in Myrmica ants from different geographic populations].

Expression of HSP70 is induced by stress factors, including sub-lethal chilling, but the role of HSP70 for overcoming consequenses of cold stress is not clear. If the role is positive, the level of HSP70 expression might be higher in populations from colder climates. By use of immunoblotting we investigated dynamics of HSP70 expression in response to cold stress in two Myrmica species from three localities of different latitude (50, 60 and 67 degrees N).

[Heat shock protein of Hsp70 in Paramecium nephridiatum and its role in adaptation to environmental salinity changes].

The level of Hsp70 was studied in the cells of eurihaline ciliate Paramecium nephridiatum after the environmental salinity changes. Two types of treatment were applied. "Shock": ciliates were placed for 1 h to the medium with stress salinity, then transferred back to the medium, they were acclimated to, for 2 h; "adaptation": ciliates were placed for 3 h into stress salinity.

[Heat shock protein of HSP70 family revealed in some contemporary freshwater Amoebae and in Acanthamoeba sp. from cysts isolated from permafrost samples].

A heat shock protein of HSP70 family was revealed for the first time in trophozoites of Acanthamoeba sp. (strain Am8) excysted from cysts previously isolated from samples of permafrost aging 30,000-35,000 years. The constitutive level of this HSP, shown by immunnoblotting in unstressed trophozoites of the ancient acanthamoebae, much surpassed that in unstressed cells of the three examined species of contemporary freshwater amebae of the genus Amoeba.

[Stylonychia lemnae as a model organism for studies of macronuclear minichromosomes of the ciliates].

The unique structural and functional organization of macronuclear (somatic nucleus) genome of the spirotrichous ciliates, exemplified by Stylonychia lemnae, has been reviewed. Data on the architecture of S. lemnae nuclear apparatus at interphase and during vegetative cell division, conjugation or autogamy are summarized.

[Heat shock proteins of freshwater protists and their involvement in adaptation to changes in the environmental salinity].

Changes in the level of heat shock proteins (HSP) in cells of freshwater protists, amoebae Amoeba proteus and ciliates Paramecium jenningsi, in response to changes in the environmental salinity were investigated. Changes in salinity levels were considered as a stress factor. The immunoblotting method revealed a polypeptide antigen cross-reacting with antibodies against bovine HSP70 in total protein extracts of both intact cells and cells subjected to salinity stress.

[Enzymes of the phosphogluconate pathway in amebas].

Glucose-6-phosphate and 6-phosphogluconate dehydrogenases (G6PD and 6PGD) are revealed in Amoeba proteus by electrophoresis in polyacrylamide gels, thus proving the availability of the phosphogluconic pathway in amoebae. 6PGD is marked as a single band, and G6PD shows multiple banding. When an amoebic homogenate is obtained using Triton-100, a supplementary form of G6PD extracted from membranes of some cell organelles (presumably mitochondria) becomes apparent.