Biomedical subjects

V N Petrov

Publications and source records attributed to V N Petrov.

At least 19 recordsLinked to original sources

PubMed2001

Cloning and characterization of TNKL, a member of tankyrase gene family.

By serological screening of a breast tumor cDNA library we have identified a novel human gene, tnkl, encoding an ankyrin-related protein with a high degree of similarity to tankyrase, the poly(ADP-ribose)polymerase associated with human telomeres (Smith et al, Science 282: 1484). The tnkl gene maps to chromosome 10, while the tnks gene encoding tankyrase is located on chromosome 8. The predicted 1166-aa protein product of the tnkl gene is 78% identical to human tankyrase and 62% to a putative D. melanogaster protein. Since the proteins have essentially identical domain structures, the corresponding genes form a distinct gene family. The possible link between TNKL and cancer justifies its further functional analysis.

Amino Acid Sequence↗

PubMed1998

[Synthesis and immunogenic properties of peptides--fragments of the immunodominant regions of the VP1 protein of the Asia-1 type of foot- and-mouth disease virus].

Potential immunodominant epitopes were predicted on the basis of a theoretical analysis of the antigenic structure of the VP1 protein of the type Asia-1 foot-and-mouth disease virus. Peptides corresponding to the 140-153, 136-153, 132-153, 143-157, 137-157, and 193-208 fragments of the VP1 protein sequence were synthesized by the solid phase method, and the immunogenic properties of the peptides were studied on guinea pigs. The shortest peptide exhibiting the protective effect was found to correspond to the, 140-153 fragment of the VP1 sequence. The Plm-(Gly)3-(140-153)-(Gly)2-Lys(Plm)-Leu and [Ac-(140-153)-(Gly)3]8-(Lys)7-Gly synthetic constructions in combination with adjuvants provided up to 80% protection of immunized animals against infection with the foot-and-mouth disease virus.

Adjuvants, Immunologic↗

PubMed1992

[Protection of naturally susceptible animals against foot-and-mouth disease with a peptide, synthesized on a lysine matrix].

A peptide VP1-(142-158)-MAP (Multiple antigen peptide system) consisting of two parts: a lysine matrix made up of three levels of lysine residues coupled with each other and amino acid sequence 142-158 of VP1 of FMD virus strain A(22)550--has been synthesized. Guinea-pigs inoculated with 20 mkg of the peptide incorporated with Freund's complete adjuvant were protected against challenge with 500 ID50 of homologous FMD virus. Sheep were immunized with a single inoculation of the peptide in a dose of 1.0 mg. Cattle inoculated twice with 1.5 mg of the peptide with incomplete adjuvant on the basis of synthetic oil developed high virus-specific antibody titres both after the first (5.3-7.6 log2 ND50/0.1 ml) and the second inoculation (10.2-11.0 log2 ND50/0.1 ml). The peptide-immunized animals were resistant to challenge with homologous virulent virus in a dose of 10(4) ID50. The immunogenic and protective capacities of the peptide VP1-(142-158)-MAP were shown to be greater as compared with those of its linear analogue-peptide VP1-(141-160).

Amino Acid Sequence↗

PubMed1991

[Protection from foot-and-mouth disease virus in naturally-susceptible animals by a linear polymer of a synthetic peptide].

Linear polymer of a peptide corresponding to the fragment 142-155 of the foot-and-mouth disease virus A22(550) protein (VP1) was synthesized. Whereas the monomeric peptide was only slightly immunogenic, the polymer induced virus-neutralizing antibodies in rabbits and protected 100% guinea pigs. Sheep vaccinated once and cattle vaccinated twice were stable against infection with the homologous virulent foot-and-mouth disease virus.

Amino Acid Sequence↗

PubMed1989

[Treatment of alcoholism by affective counterattribution].

A new narcopsychotherapeutic technique termed "affective counterattribution" (ACA) is offered to treat alcohol addiction. The use of ACA increased the effectiveness of alcoholism treatment that was ensured by association of strong pharmacogenic negative emotional experience coupled with bright hallucinatory images to notions of alcohol and alcohol-related stimuli. Alcoholic attitude was destroyed and the patients' pathological personality traits were corrected.

Abreaction↗

PubMed1987

[Decrease in the concentration of leukocyte acetylation coenzyme associated with vitamin precursor deficiency in patients with alcoholic delirium].

Sixty-three patients with the typical variant of delirium tremens were examined. The results showed a marked reduction (by 8.7 times) in levels of coenzyme A (CoA) in leukocytes, which was indicative of deficiency of the coenzymic form of pantothenic acid (PA). Changes in CoA concentrations in leukocytes observed at the height of psychosis in patients with alcoholic delirium as compared to other parameters of PA metabolism have great significance for the assessment of vitamin metabolism. PA deficiency was more expressed in cases of long-standing and massive alcoholization which induces an earlier development of psychosis. CoA levels in leukocytes may be used as a parameter of detoxication processes in patients with delirium tremens. The data obtained are considered as indication for administration of PA drugs in combined detoxifying therapy of alcoholic psychoses.

Adult↗

PubMed1986

[Multiplicity of affinity modification of RNAse during its alkylation with a reactive analog of 5-deoxyribonucleotide].

The interaction of pancreatic RNase with 5'-deoxyribodinucleotide alkylating derivative, 4-(N-2-chloroethyl-N-methylamino)benzylamide of d(pTpA) d[(ClRCH2NH)pTpA], was studied. The unreactive oxyanalogue d[(HORCH2NH)pTpA] was shown to act as competitive inhibitor of cCMP hydrolysis by RNase. d[(ClRCH2NH)pTpA] irreversibly inactivated RNase. A protective effect was exerted by d(pTpA) and d[(HORCH2NH)pTpA]. The modification, although having an affinity character, was not accompanied by total inactivation of the enzyme. It was supposed that covalent bonding between the reagent and enzyme induced the dinucleotide displacement from the recognition site. The formation of four RNase monolabeled forms retaining the activity in the hydrolysis of cCMP and poly(U) was demonstrated.

Alkylating Agents↗

PubMed1984