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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)
Changes in polymerization degree of actin of newborn and adult rabbit muscles while storing solutions were studied. It is found that under different polymerization and storage conditions including the presence of ATP, Ca++ ions, 2-metacaptoethanole of ethanole which slow down the inactivation of actin the latter proceeds faster in newborn rabbits than in(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)
Hydrolysis of the C-peptide from recombinant human proinsulin, porcine insulin, and melittin by the E. coli actin-degrading proteinase ECP 32 was studied by reverse phase high performance liquid chromatography and mass spectrometry with electrospray ion source. Proteinase ECP 32 hydrolyzed only melittin at the Ala15-Leu16 or Leu16-Ile17 bonds (KM = 2.4 x(More)
New analytical possibilities of biological macromolecule partition in a two-phase polymer system (dextran-500/polyethyleneglycol-6000) were investigated. The technical principles were based on the fact that optical density of the system changes during phase formation. Various actin forms were investigated. Unlike G-actin, F-actin increases the speed of(More)