S Iu Khaĭtlina

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Effect of antioxidants on actin cytoskeleton in 3T3 fibroblasts and 3T3 fibroblasts transformed with SV40 virus (3T3-SV40 cells) was studied. Antioxidants used were as follows: N-acetyl-L-cysteine (NAC), (-)-2-oxo-4-thiazolidine-carboxylic acid (OTZ), and glutathione in the reduced form (GSH). Both NAC and OTZ are precursors of GSH in the cell, but, in(More)
A novel bacterial protease specifically hydrolyzing actin with the formation of a stable fragment with Mr of 36 kDa was obtained. This protease was shown to be synthesized at the stationary phase of bacterial culture growth. The actin hydrolysis by bacterial protease was inhibited by o-phenanthroline, EDTA and p-chloromercuribenzoate but not by(More)
Bacteria of spontaneously isolated non-pathogenic strain E. coli A2 have been previously shown to produce a new proteinase, referred to as protease ECP 32, which specifically cleaves actin (Khaitlina et al., 1988; Matveyev et al., 1996). Similar proteinase activity was found in revertants of Shigella flexneri L-forms. In this work immunofluorescence and(More)
Immunocytochemical analysis of preparation of dispersed nuclei content in oocytes of III-IV stages of oogenesis, in terms of Dumont (1972), from hibernating grass frogs using monoclonal antibodies against actin, revealed two types of intranuclear structures containing this protein: coiled bodies (CB) and satellite microbodies (SM). Staining of these(More)
Actin preparation from skeletal muscles of new-born, 10 days old and adult rabbits, containing less than or equal to 5% of inactivated actin and 1-2% of other myofibrillar proteins, were studied by means of flow birefringence and viscosimetry. It is found, that, like earlier studied crude preparations, purified actin preparations, isolated at different(More)
The proteolysis-stable actin fragment (m. w. 36300 as determined by SDS polyacrylamide gel electrophoresis) was obtained by actin treatment with a non-identified bacterial protease. This fragment is larger than the trypsin-stable actin fragment and is similar to the unstable trypsin intermediate fragment. The obtained actin fragment is not polymerized, does(More)
The mode of tryptophan residue orientation in myosin and action myofilaments of the muscle fiber was studied using polarized ultraviolet (UV) fluorescent microscopy of the muscle fiber was studied using polarized ultraviolet (UV) fluorescent microscopy technique. During an elective extraction of proteine from thick and thin myofillaments changes in UV(More)