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T V Gupalova

Publications and source records attributed to T V Gupalova.

11 recordsLinked to original sources
PubMed2005

[The light diffusion technique for estimation of the size of urine particles in patients with type 2 diabetes mellitus in the Tamm-Horsfall protein precipitation].

Tamm-Horsfall uroprotein accounts for more than 50% of the urinary proteins in healthy individuals. In abnormalities, it creates a favorable background for detecting smaller-sized uroproteins and for diagnosing pathological processes from the results of native urine tests. In this connection, there is a need for precipitating Tamm-Horsfall glycoprotein while applying laser correlation spectroscopy to analyze the size of urine particles in patients with type 2 diabetes mellitus. Eighty patients with this condition concurrent with different stages of diabetic nephropathy and 23 apparently healthy individuals were examined. The findings suggest that the subfraction urine composition before and after Tamm-Horsfall protein precipitation is different in apparently healthy individuals and patients with type 2 diabetes mellitus concurrent with diabetic nephropathy. This is most likely to be due to the change in the qualitative composition of protein as renal lesion progresses, to the specific features of protein excretion at different stages of a pathological process, and to different concentrations of other low and high molecular-weight proteins.

Adult↗
PubMed2002

Quantitative investigation of the affinity properties of different recombinant forms of protein G by means of high-performance monolithic chromatography.

The recombinantly produced different forms of protein G, namely monofunctional immunoglobulin G (IgG) binding, monofunctional serum albumin (SA) binding and bifunctional IgG/SA binding proteins G, are compared with respect to their specific affinities to blood IgG and SA. The affinity mode of the recently developed high-performance monolithic disk chromatography has been used for fast quantitative investigations. Using single affinity disks as well as two discs stacked into one separation unit, one order of magnitude in adsorption capacities for IgG and SA were found both for monofunctional and bifunctional protein G forms used as specific affinity ligands. However, despite the adsorption difference observed, the measured dissociation constants of the affinity complexes seemed to be very close. The analytical procedure developed can be realized within a couple of minutes. Up-scaling of the developed technology was carried out using another type of monolithic materials, i.e. CIM affinity tubes.

Adsorption↗
PubMed1997

[The detection of microalbuminuria by using a recombinant albumin receptor].

Methods of ELISA competitive binding and blotting on nitrocellulose membranes were developed for detecting microalbuminuria in diabetic nephropathy. These methods are based on the use of recombinant albumin receptor. They are highly specific and sensitive and are recommended for everyday clinical use.

Albuminuria↗
PubMed1996

[Obtaining and properties of recombinant protein G].

A gene for G protein from Streptococcus strain G148 was cloned in Escherichia coli, which gave rise to several plasmids. One plasmid containing a 1.5 kb insert coding for entire G protein with 63 kD. This protein had both an IgG binding capacity and albumin-binding activity. The second plasmid containing a 0.7 kD insert coded for protein with MM of 38 kD and had only an IgG-binding activity. The third coding for protein with 25 kD has only albumin-binding activity. After subcloning the 1.5-kb insert into the other vector pSP65 and analysing the nucleotide sequence of this insert both in pSP65 vector, the authors came to the conclusion that the proteins obtained are fusion protein of G protein and beta-galactosidase. All the proteins were prepared by affinity chromatography on IgG sepharose or on HSA sepharose. The interaction between G protein and polyclonal and monoclonal IgG of the reactions between G protein and human IgG have determined.

Blotting, Western↗
PubMed1989

[Creation and analysis of a bank of chromosomal genes of Streptococcus group A].

The representative genomic library of chromosomal genes has been constructed for streptococcus group A serotype M48 strain 1/64 on the vector lambda L 47.1. Screening of the obtained genomic library by hybridization and immunological techniques revealed about 50 clones producing the streptococcal antigens (extracellular nonidentified products and non-type specific structural streptococcal proteins). Among the recombinant clones three were found to harbour the genetic determinants for M-protein. One the clones contains a determinant coding for epitopes crossreacting with antisera to M-proteins of other serotypes and a protective epitope. The presence of the latter was tested in an indirect bactericidal test.

Animals↗
PubMedDate not supplied

[Comparative characteristics of protein G gene in Streptococci of groups C and G isolated from humans].

The treatment of streptococci, groups C and G, with bromocyanogen made it possible to isolate surface G protein, capable of binding human serum albumin (HSA) and polyclonal IgG. In this work the presence of G protein in all staphylococcal strains, groups C and G, is shown. The differences between the strains by the level of expression, molecular weight and functional activity of G protein, extracted from streptococci of groups C and G, permitted the identification of 3 groups of strains, containing the molecules of G protein with different numbers of IgG- and HSA-binding domains: with 3 IgG- and HSA-binding domains, with 2 IgG- and HSA-binding domains and with only 2 IgG-binding domains. Each strain under study expressed only one of the molecule of G protein. The work shows the possibility of the identification of streptococci, groups C and G, by the molecular characteristics of G proteins themselves and their respective coding genes.

Bacterial Proteins↗
PubMedDate not supplied

[Isolation and characteristics of plasmids determining multiple antibiotic resistance in strains of group A streptococci].

DNA of the streptococcal plasmid ERLI, determining resistance to erythromycin and lincomycin has been studied. The presence of satellite DNA component in streptococcal DNA has been demonstrated by dye-CsCl and CsCl density centrifugation, by chromatography of denatured-renatured DNA on the nitrocellulose and by electron microscopy. By all these methods the presence of covalently closed circular DNA molecules has been shown. Plasmid DNA has buoyant density in CsCl equal to 1.698 g/cm3 (GC content--38.8%), molecular weight (by electron microscopy) -- 19.8 Mdal; number of copies chromosomal genome equivalent is equal to about 4--4.5. Plasmid ERLI DNA was extracted from an original strain-carrier of plasmid ERLI, from a transduced strain which received plasmid ERLI as a result of transduction and lysogenization by phage "mo" and from the two antibiotic sensitive EMS mutants of resistant strain. Satellite DNA could not be isolated from a sensitive strain which served as a recipient in transduction experiments. The results obtained are in agreement with the literature on the molecular weight of the plasmid measured by the sedimentation analysis and with the previous genetic data on the antibiotic resistance within group A streptococci.

Centrifugation, Density Gradient↗